Recent and Selected

Pedersen, B.P., Kumar, H., Waight, A.B., Risenmay, A., Roe-Zurz, Z., Chau, B., Schlessinger, A., Harries, W., Sali, A., Johri, K., Stroud, R.M. (2013). Crystal structure of a eukaryoticphosphate transporter.  Nature. (PMID: 23542591)
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Pieper, U., Schlessinger, A., Kloppmann, E., Chang, G.A., Chou, J.J., Dumont, M.E., Fox, B.G., Fromme, P., Hendrickson, W.A., Malkowski, M.G., Rees, D.C., Stokes, D.L., Stowell, M.H., Wiener, M.C., Rost, B., Stroud, R.M., Stevens, R.C., Sali, A. (2013). Coordinating the impact of structural genomics on the human α-helical transmembrane proteome. Nat Struct Mol Biol 20: 135-8. (PMID: 23381628/PMCID: in process).
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Pozzi, C., Ferrari, S., Cortesi, D., Luciani, R., Stroud, R.M., Catalano, A., Costi, M.P., Mangani, S. (2012). The structure of Enterococcus faecalis thymidylate synthase provides clues about folate bacterial metabolism. Acta Crystallogr D Biol Crystallogr 68: 1232-41. (PMID: 22948925)
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Egea, P.F., Muller-Steffner, H., Kuhn, I., Cakir-Kiefer, C., Oppenheimer, N.J., Stroud, R.M., Kellenberger, E., Schuber, F. (2012). Insights into the mechanism of bovine CD38/NAD+glycohydrolase from the X-ray structures of its michaelis complex and covalently-trapped intermediates. PLoS One 7(4):e34918. (PMCID: PMC3329556)
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Wu, S., Avila-Sakar, A., Kim, J., Booth, D.S., Greenberg, C.H., Rossi, A., Liao, M., Li, X., Alian, A., Griner, S.L., Juge, N., Yu, Y., Mergel, C.M., Chaparro-Riggers, J., Strop, P., Tampe, R., Edwards, R.H., Stroud, R.M., Craik, C.S., Cheng, Y. (2012) Fabs enable single particle cryoEM studies of small proteins. Structure 20: 582-92. PMCID: PMC3322386
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Varrin-Doyer, M., Spencer, C.M., Schulze-Topphoff, U., Nelson, P.A., Stroud, R.M., Cree, B.A., Zamvil, S.S. (2012). Aquaporin 4-specific T cells in neuromyelitis optica exhibit a Th17 bias and recognize Clostridium ABC transporter. Ann Neurol 72: 53-64. (PMCID: PMC3405197)
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Wang, Z., Abeysinghe, T., Finer-Moore, J.S., Stroud, R.M., Kohen, A. (2012). A Remote Mutation Affects the Hydride Transfer by Disrupting Concerted Protein Motions in Thymidylate Synthase. J Am Chem Soc 134: 17722-30. PMCID: PMC3490427
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Metzger, L.E., Lee, J.K., Finer-Moore, J.S., Raetz, C.R., Stroud, R.M. (2012). LpxI structures reveal how a lipid A precursor is synthesized. Nat Struct Mol Biol 19: 1132-1138. (PMCID: PMC3562136)
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Carosati, E., Tochowicz, A., Marverti, G., Guaitoli, G., Benedetti, P., Ferrari, S., Stroud, R.M., Finer-Moore, J., Luciani, R., Farina, D., Cruciani, G., Costi, M.P. (2012). Inhibitor of ovarian cancer cells growth by virtual screening: a new thiazole derivative targeting human thymidylate synthase. J Med Chem 55: 10272-6. (PMID: 23075414/ PMCID: in process).
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Chaudhary, S., Pak, J.E., Gruswitz, F., Sharma, V., Stroud, R.M. (2012). Overexpressing Human Membrane Proteins in Stably Transfected and Clonal Human Embryonic Kidney 293S Cells. Nature Protocols
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Chaudhary, S., Pak, J.E., Pedersen, B.P., Bang, L.J., Zhang, L.B., Ngaw, S.M., Green, R.G.,
Sharma, V., Stroud, R.M. (2011). Efficient expression screening of human membrane proteins in transiently transfected Human Embryonic Kidney 293S cells. Methods. (PMID: 21925269)
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Korennykh, A.V., Egea, P.F., Korostelev, A.A., Finer-Moore, J., Stroud, R.M., Zhang, C., Shokat,
K.M., Walter, P.  (2011). Cofactor-mediated conformational control in the bifunctional kinase/RNase Ire1. BMC Biol 9: 48. (PMID: 21729334)
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Korennykh, A.V., Korostelev, A.A., Egea, P.F., Finer-Moore, J., Stroud, R.M., Zhang, C., Shokat,
K.M., Walter, P. (2011). Structural and functional basis for RNA cleavage by Ire1. BMC Biol 9: 47. (PMID: 21729333)
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Kim, J., Stroud, R.M., Craik, C.S. (2011). Rapid identification of recombinant Fabs that bind to
membrane proteins.  Methods, epub ahead of print, Sept. 20. (PMID: 21958987)
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Stroud, R.M. (2011). New tools in membrane protein determination. F1000 Biol Rep. 3:8.
(PMCID: 3100781).
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Stroud, R.M., Schertler, G.F. (2011). Membranes. Curr Opin Struct Biol.  21, 495-6.
(PMID: 21875531).
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Rosenberg, O.S., Dovey, C., Tempesta, M., Robbins, R.A., Finer-Moore, J.S., Stroud, R.M., Cox,
J.S.  (2011). EspR, a key regulator of Mycobacterium tuberculosis virulence, adopts a unique dimeric structure among helix-turn-helix proteins. Proc Natl Acad Sci USA. (PMID: 21795602)
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New tools in membrane protein determination Stroud, R.M. F1000 Biology Reports (April 2011); 3:8. Download (PDF)

Overexpression and Purification of Integral Membrane Proteins in Yeast Methods in Enzymology. Hays F, Roe-Zurz Z, Stroud R. M. (2010). Chapter 29 p 697-709. PMID: 20946832. Download (PDF)

Metal induced conformational changes in ZneB sugest an active role of membrane fusion proteins in efflux resistance systems. Fabien De Angelis*, John K. Lee*, Joseph D. O'Connell III, Larry J. Miercke, Koen H. Verschueren, Vasundara Srinivasan, Cedric Bauvois, Cedric Govaerts, Rebecca A. Robbins, Jean-Marie Ruysschaert, Robert M. Stroud, and Guy Vandenbussche. PNAS (June 2010); 107: 11038-11043. *equal contribution Download (PDF)

Function of human Rh based on structure of RhCG at 2.1 Å. Franz Gruswitz, Sarika Chaudhary, Joseph D. Ho, Avner Schlessinger, Bobak Pezeshki, Chi-Min Ho, Andrej Sali, Connie M. Westhoff, and Robert M. Stroud. PNAS (May 2010); 107. Download (PDF)

Catalytically-active complex of HIV-1 integrase with a viral DNA substrate binds anti-integrase drugs. Akram Alian, Sarah L. Griner, Vicki Chiang, Manuel Tsiang, Gregg Jones, Gabriel Birkus, Romas Geleziunas, Andrew D. Leavitt, and Robert M. Stroud
PNAS, (May 2009); 106: 8192-8197. Download (PDF)

Crystal structure of human aquaporin 4 at 1.8 Å and its mechanism of conductance. Joseph D. Ho, Ronald Yeh, Andrew Sandstrom, Ilya Chorny, William E. C. Harries, Rebecca A. Robbins, Larry J. W. Miercke, and Robert M. Stroud PNAS, (May 2009); 106: 7437-7442. Download (PDF)

The unfolded protein response signals through high-order assembly of Ire1. Alexei V. Korennykh, Pascal F. Egea, Andrei A. Korostelev, Janet Finer-Moore, Chao Zhang, Kevan M. Shokat, Robert M. Stroud and Peter Walter. (2009) Nature 457, 687-93.

Selecting optimum eukaryotic integral membrane proteins for structure determination by rapid expression and solubilization screening. Min Li, Frank A Hays, Zygy Roe-Zurz, Linda Vuong, Libusha Kelly, Chi Min Ho, Rebecca M Robbins, Ursula Pieper, Joseph O'Connell III, Larry J Miercke, Kathleen M Giacomini, Andrej Sali, and Robert M Stroud. (2009) J Mol Biol 385(3); 820-30.

Ratiocinative screen of eukaryotic integral membrane protein expression and solubilization for structure determination. Franklin A Hays, Zygy Roe-Zurz, Min Li, Libusha Kelly, Franz Gruswitz, Andrej Sali, and Robert M Stroud. (2008) J Struct Funct Genomics.

Crystal structure of bovine mitochondrial factor B at 0.96-Å resolution. John K. Lee, Grigory I. Belogrudov, and Robert M. Stroud (2008) PNAS 105; 13379-84.
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Crystal structure of the aquaglyceroporin PfAQP from the malarial parasite Plasmodium falciparum. Zach E. Newby, Josepeh O'Connell III, Yaneth Robles-Colmenares, Shahram Khademi, Larry J. Miercke, and Robert M. Stroud. (2008) Nat Struct Mol Biol 15(6); 619-25.
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Structure of a TrmA–RNA complex: A consensus RNA fold contributes to substrate selectivity and catalysis in m5U methyltransferases. Akram Alian, Tom T. Lee, Sarah L. Griner, Robert M. Stroud, and Janet Finer-Moore. (2008) PNAS 105; 6876-6881.
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Structural and biochemical insights into the dicing mechanism of mouse Dicer: A conserved lysine is critical for dsRNA cleavage. Zhihua Du, John K. Lee, Richard Tjhen, Robert M. Stroud, and Thomas L. James. (2008) PNAS 105; 2391-2396.
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TARP Auxiliary Subunits Switch AMPA Receptor Antagonists into Partial Agonists. Karen Menuz, Robert M. Stroud, Roger A. Nicoll, Franklin A. Hays. (2007) Science 318; 815-817.
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Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96Å. Franz Gruswitz, Joseph O'Connell, III, and Robert M. Stroud. (2007) PNAS 104; 42-47.
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The Role of Protein Dynamics in Thymidylate Synthase Catalysis: Variants of Conserved 2'-Deoxyuridine 5'-Monophosphate (dUMP)-Binding Tyr-261. Zachary Newby, Tom T. Lee, Richard J. Morse, Yaoquan Liu, Lu Liu, Prasanna Venkatraman,
Daniel V. Santi, Janet S. Finer-Moore, and Robert M. Stroud. (2006) Biochemistry Vol 45, 24.
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Substrate Recognition by RNA 5-Methyluridine Methyltransferases and Pseudouridine Synthases: A Structural Perspective. Sun Hur, Robert M. Stroud, and Janet Finer-Moore. (2006) The Journal of Biological Chemistry Vol. 281, No. 51, pp. 38969–38973.
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The Structure of a Ketoreductase Determines the Organization of the b-Carbon Processing Enzymes of Modular Polyketide Synthases. Adrian T. Keatinge-Clay, and Robert M. Stroud. (2006) Structure 14, 737–748.
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Gas Channels for Ammonia. Khademi, S., and Stroud,R.M. (2006), Invited Chapter in Royal Society of Chemistry: Structural Biology of Membrane Proteins, ed., Reinhard Grisshammer and Susan K. Buchanan. Chapter 12, 212-234.

The Amt/MEP/Rh family: structure of AmtB and the mechanism of ammonia gas conduction. Khademi, S., and Stroud, R.M. (2006) Physiology (Bethesda)21: 419-429.

Aquaporins: Integral Membrane Channel Proteins. Stroud, R.M., Harries, W.E.C., Lee, J, Khademi, S., and Savage, D (2006), Invited Chapter  in Royal Society of Chemistry: Structural Biology of Membrane Proteins, ed., Reinhard Grisshammer and Susan K. Buchanan. Chapter 11, 195-211.

On the Mechanism of Sensing Unfolded Protein in the Endoplasmic Reticulum.Credle, J.J., Finer-Moore, J.S., Papa, F.R., Stroud, R.M. and Walter, P. (2005) Proc Nat Acad Sci  102, 18773-18784

Structural Basis for Conductance by the Archaeal Aquaporin AqpM at 1.68Å. Lee, J.K., Stroud, R.M.  (2005) Proc. Nat Acad Sci U S A 102, 18932-7.

A unique RNA fold in the rumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function. Lee, T., Agarwalla, S., Stroud, R.M. (2005) Cell 120, 599-611.
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Targeting proteins to membranes: structure of the signal recognition particle. Egea, P.F., Stroud, R.M., Walter, P. (2005) Current Opinion in Structural Biology 15:213-220.
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De novo design of an IL-4 antagonist and its structure at 1.9Å. LaPorte, S.L., Forsyth, C.M., Cunningham, B.C., Miercke, L.J., Akhaven, D., Stroud, R.M. (2004) PNAS vol 102 no.6 1889-1894.
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Mechanism of association and reciprocal activation of two GTPases. Shan, S. O., Stroud, R. M., Walter, P. (2004) PLoS Biol 2, e320
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Structure of Human Pro-Chymase: A Model for the Activating Transition of Granule Associated Proteases. Reiling, K.K Krucinski, J. Miercke,L.J.W. Raymond, W.W., Caughey, G.H. Stroud, R.M. (2003) Biochemistry 42, 2616-2624. PDB accession No. 1NN6
Review abstract
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Conformational Dynamics Along an Enzymatic Reaction Pathway: Thymidylate Synthase, ‘the Movie.’ Robert M. Stroud, Janet S. Finer-Moore (2003) Biochemistry 42, 239-247. (web released Dec 17th 2002 Bi 020598i)
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Anisotropic Dynamics of the JE-2147-HIV Protease complex: Drug Resistance and Thermodynamic Binding Mode Examined in a 1.09Å Structure. Reiling, K., Endres, N., Dauber, D., Craik, C., Stroud, R. (2002) Biochemistry 41 No 14 4582 –4594.
PDB accession No. 1KZK
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Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthases: Versatility from a unique substrate channel. Tsai, S.-C., Miercke, L.J.W., Krucinski, J., Gokhale, R., Chen, Julian C.-H., Foster, P.G., Cane, D.E., Khosla, C., and Stroud, R.M. (2001). PNAS 98 26 14808-14813.
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Crystal Structure of the HIV-1 Integrase Catalytic Core and C-Terminal Domains Presents a Model for Viral DNA Binding. Chen, J. C.-H., Krucinski, J., Miercke, L.J.W., Finer-Moore, J.S., Tang, A.H., Leavitt, A.D., and Stroud, R.M. (2000) Proc. of Natl. Acad. Sci. 97, 15 8233-8238.
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Functional consequences of the Kaposi's Sarcoma-associated herpesviral protease structure: Regulation of activity and dimerization by conserved structural elements. Reiling, K.K., Pray, T.R., Craik, C.S., and Stroud, R.M. (2000) Biochemistry 39, 42 12796-803.
Review abstract
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Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+ GDP.
Freyman, DM; Keenan, RJ; Stroud, RM; and Walter, P. (1999) Nature Structural Biology 6, 793-801. PDB Accession Nos. 1NG1, 2NG1 , 3NG1
Review abstract
View PDB structure 1NG1, 2NG1, 3NG1
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