1gbm
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(New page: 200px<br /><applet load="1gbm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gbm, resolution 2.28Å" /> '''ALPHA-LYTIC PROTEASE...)
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Revision as of 13:47, 20 November 2007
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ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE 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.
About this Structure
1GBM is a Single protein structure of sequence from Lysobacter enzymogenes with SO4 as ligand. This structure superseeds the now removed PDB entry 1P08. Active as Alpha-lytic endopeptidase, with EC number 3.4.21.12 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
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