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1gbe
From Proteopedia
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|PDB= 1gbe |SIZE=350|CAPTION= <scene name='initialview01'>1gbe</scene>, resolution 2.30Å | |PDB= 1gbe |SIZE=350|CAPTION= <scene name='initialview01'>1gbe</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </span> |
|GENE= ALPHA-LYTIC PROTEASE PREPROENZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69 Lysobacter enzymogenes]) | |GENE= ALPHA-LYTIC PROTEASE PREPROENZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69 Lysobacter enzymogenes]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbe OCA], [http://www.ebi.ac.uk/pdbsum/1gbe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gbe RCSB]</span> | ||
}} | }} | ||
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[[Category: Agard, D A.]] | [[Category: Agard, D A.]] | ||
[[Category: Mace, J E.]] | [[Category: Mace, J E.]] | ||
| - | [[Category: SO4]] | ||
[[Category: active-site mutation]] | [[Category: active-site mutation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:40:47 2008'' |
Revision as of 17:40, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | ALPHA-LYTIC PROTEASE PREPROENZ (Lysobacter enzymogenes) | ||||||
| Activity: | Alpha-lytic endopeptidase, with EC number 3.4.21.12 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU
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
1GBE is a Single protein structure of sequence from Lysobacter enzymogenes. 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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