1p01
From Proteopedia
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| , resolution 2.0Å | |||||||
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| Ligands: | , , | ||||||
| Activity: | Alpha-lytic endopeptidase, with EC number 3.4.21.12 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SERINE PROTEASE MECHANISM. STRUCTURE OF AN INHIBITORY COMPLEX OF ALPHA-LYTIC PROTEASE AND A TIGHTLY BOUND PEPTIDE BORONIC ACID
Overview
The structure of the complex formed between alpha-lytic protease, a serine protease secreted by Lysobacter enzymogenes, and N-tert-butyloxycarbonylalanylprolylvaline boronic acid (Ki = 0.35 nM) has been studied by X-ray crystallography to a resolution of 2.0 A. The active-site serine forms a covalent, nearly tetrahedral adduct with the boronic acid moiety of the inhibitor. The complex is stabilized by seven hydrogen bonds between the enzyme and inhibitor with additional stabilization arising from van der Waals interactions between enzyme and inhibitor side chains and the burying of 330 A2 of hydrophobic surface area. Hydrogen bonding between Asp-102 and His-57 remains intact in the enzyme-inhibitor complex, and His N epsilon 2 is well positioned to donate its hydrogen to the leaving group. Little change in the positions of protease residues was observed on complex formation (root mean square main chain deviation = 0.13 A), suggesting that in its native state the enzyme is complementary to tetrahedral reaction intermediates or to the nearly tetrahedral transition state for the reaction.
About this Structure
1P01 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Serine protease mechanism: structure of an inhibitory complex of alpha-lytic protease and a tightly bound peptide boronic acid., Bone R, Shenvi AB, Kettner CA, Agard DA, Biochemistry. 1987 Dec 1;26(24):7609-14. PMID:3122831
Page seeded by OCA on Sun Mar 30 22:52:53 2008
