1gbe

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[[Image:1gbe.jpg|left|200px]]
[[Image:1gbe.jpg|left|200px]]
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{{Structure
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|PDB= 1gbe |SIZE=350|CAPTION= <scene name='initialview01'>1gbe</scene>, resolution 2.30&Aring;
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The line below this paragraph, containing "STRUCTURE_1gbe", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE= ALPHA-LYTIC PROTEASE PREPROENZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69 Lysobacter enzymogenes])
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|DOMAIN=
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{{STRUCTURE_1gbe| PDB=1gbe | SCENE= }}
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|RELATEDENTRY=
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|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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'''ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU'''
'''ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU'''
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[[Category: Agard, D A.]]
[[Category: Agard, D A.]]
[[Category: Mace, J E.]]
[[Category: Mace, J E.]]
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[[Category: active-site mutation]]
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[[Category: Active-site mutation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:22:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:40:47 2008''
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Revision as of 14:22, 2 May 2008

Image:1gbe.jpg

Template:STRUCTURE 1gbe

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 Page seeded by OCA on Fri May 2 17:22:41 2008

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