This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1p01

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1p01.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1p01.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1p01| PDB=1p01 | SCENE= }}
{{STRUCTURE_1p01| PDB=1p01 | SCENE= }}
-
'''SERINE PROTEASE MECHANISM. STRUCTURE OF AN INHIBITORY COMPLEX OF ALPHA-LYTIC PROTEASE AND A TIGHTLY BOUND PEPTIDE BORONIC ACID'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_3122831}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 3122831 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_3122831}}
==About this Structure==
==About this Structure==
Line 24: Line 28:
[[Category: Agard, D A.]]
[[Category: Agard, D A.]]
[[Category: Bone, R.]]
[[Category: Bone, R.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:30:22 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:37:36 2008''

Revision as of 11:37, 29 July 2008

Image:1p01.png

Template:STRUCTURE 1p01

SERINE PROTEASE MECHANISM. STRUCTURE OF AN INHIBITORY COMPLEX OF ALPHA-LYTIC PROTEASE AND A TIGHTLY BOUND PEPTIDE BORONIC ACID

Template:ABSTRACT PUBMED 3122831

About this Structure

1P01 is a Single protein structure. 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 Tue Jul 29 14:37:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p01"
Personal tools