α-lytic protease PDB codes

*bracketed id codes are no longer available from the PDB.

References

Bone, R, Shenvi, AB, Kettner, CA, Agard, DA (1987) Serine Protease Mechanism: Structure of an Inhibitory Complex of a-Lytic Protease and a Tightly Bound Peptide Boronic Acid. Biochemistry 26: 7609.

Bone, R, Silen, JL, Agard, DA (1989) Structural Plasticity Broadens the Specificity of an Engineered Protease. Nature 339: 191.

Bone, R, Frank, D, Kettner, CA, Agard, DA (1989) Structural Analysis of Specificity: a-Lytic Protease Complexes with Analogues of Reaction Intermediates. Biochemistry 28: 7600.

Bone, R, Sampson, NS, Bartlett, PA, Agard, DA (1991a) Crystal Structures of a-Lytic Protease Complexes with Irreversibly Bound Phosphonate Esters. Biochemistry 30: 2263.

Bone, R, Fujishige, A, Kettner, CA, Agard, DA (1991b) Structural Basis for Broad Specificity in a-Lytic Protease Mutants. Biochemistry 30: 10388.

Fuhrmann, CN, Brian A. Kelch, Nobuyuki Ota and David A. Agard, The 0.83 Å Resolution Crystal Structure of a-Lytic Protease Reveals the Detailed Structure of the Active Site and Identifies a Source of Conformational Strain. Journal of Molecular Biology, (2004), 338(5), 999-101 (pdf)

Fuhrmann, C.N., Daugherty, M.D., and Agard, D.A., "Subangstrom Crystallography Reveals that Short Ionic Hydrogen Bonds, and Not a His-Asp Low-Barrier Hydrogen Bond, Stabilize the Transition State in Serine Protease Catalysis," JACS, 2006, 128(28), 9086-102 (pdf)

Fujinaga, M, Delbaere, LTJ, Brayer, GD, James, MNG (1985) Refined Structure of a-Lytic Protease 1.7Å resolution: Analysis of Hydrogen Bonding and Solvent Structure. J Mol Biol 131: 479.

Kelch, BA and Agard, DA, "Mesophile versus Thermophile: Insights Into the Structural Mechanisms of Kinetic Stability," J. Mol. Biol., 2007, 370(4), 784-95 (pdf)

Kelch, BA, Eagen, KP, Erciyas, FP, Humphris, EL, Thomason, AR, Mitsuiki, S and Agard, DA, "Structural and Mechanistic Exploration of Acid Resistance: Kinetic Stability Facilitates Evolution of Extremophilic Behavior," Journal of Molecular Biology, (2007), 368(3), 870-883 (pdf)

Kelch BA, Salimi NL, Agard DA., "Functional modulation of a protein folding landscape via side-chain distortion." Proc Natl Acad Sci U S A. (2012), 109(24), 9414-9.(pdf)

Mace, JE, Agard, DA (1995) Kinetic and Structural Characterization of Mutations of Glycine 216 in a-Lytic Protease: A New Target for Engineering Substrate Specificity. J Mol Biol 254: 720.

Rader, SD, Agard, DA (1997) Conformational Substates in Enzyme Mechanism: The 120K Structure of a-Lytic Protease at 1.5Å Resolution. Protein Science 6: 1375.

Peters, RJ et al (1998) Pro Region C-terminus: Protease Active Site Interactions Are Critical in Catalyzing the Folding of a-Lytic Protease. Biochemistry 37: 12058.

Sauter, NK, Mau, T, Rader, SD, Agard, DA (1998) Structure of a-Lytic Protease Complexed with its Pro Region. Nature Structural Biology 5: 945.