1gbl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1gbl.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1gbl.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1gbl| PDB=1gbl | SCENE= }}
{{STRUCTURE_1gbl| PDB=1gbl | SCENE= }}
-
'''ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID'''
+
===ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID===
-
==Overview==
+
<!--
-
Gly216 in the active site of the broadly specific MA190 mutant of alpha-lytic protease has been found to be remarkably tolerant of amino acid substitutions. Side-chains as large as Trp can be accommodated within the substrate-binding pocket without abolishing catalysis, and have major effects upon the substrate specificity of the enzyme. Kinetic characterization of eleven enzymatically active mutants against a panel of eight substrates clearly revealed the functional consequences of the substitutions at position 216. To understand better the structural basis for their altered specificity, the GA216 + MA190 and GL216 + MA190 mutants have been crystallized both with and without a representative series of peptide boronic acid transition-state analog inhibitors. An empirical description and non-parametric statistical analysis of structural variation among these enzyme: inhibitor complexes is presented. The roles of active site plasticity and dynamics in alpha-lytic protease function and substrate preference are also addressed. The results strongly suggest that substrate specificity determination in alpha-lytic protease is a distributed property of the active site and substrate molecule.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7500345}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7500345 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7500345}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Active-site mutation]]
[[Category: Active-site mutation]]
[[Category: Inhibitor complex]]
[[Category: Inhibitor complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:23:00 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:02:20 2008''

Revision as of 02:02, 1 July 2008

Image:1gbl.png

Template:STRUCTURE 1gbl

ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID

Template:ABSTRACT PUBMED 7500345

About this Structure

1GBL is a Single protein structure of sequence from Lysobacter enzymogenes. This structure supersedes the now removed PDB entry 4lpr. Full crystallographic information is available from OCA.

Reference

Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity., Mace JE, Agard DA, J Mol Biol. 1995 Dec 8;254(4):720-36. PMID:7500345

Page seeded by OCA on Tue Jul 1 05:02:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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