1hay: Difference between revisions
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|PDB= 1hay |SIZE=350|CAPTION= <scene name='initialview01'>1hay</scene>, resolution 1.7Å | |PDB= 1hay |SIZE=350|CAPTION= <scene name='initialview01'>1hay</scene>, resolution 1.7Å | ||
|SITE= <scene name='pdbsite=CAT:Active+Site+Catalytic+Triad'>CAT</scene> | |SITE= <scene name='pdbsite=CAT:Active+Site+Catalytic+Triad'>CAT</scene> | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/ | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hay OCA], [http://www.ebi.ac.uk/pdbsum/1hay PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hay RCSB]</span> | |||
}} | }} | ||
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==Reference== | ==Reference== | ||
X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate., Wilmouth RC, Edman K, Neutze R, Wright PA, Clifton IJ, Schneider TR, Schofield CJ, Hajdu J, Nat Struct Biol. 2001 Aug;8(8):689-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11473259 11473259] | X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate., Wilmouth RC, Edman K, Neutze R, Wright PA, Clifton IJ, Schneider TR, Schofield CJ, Hajdu J, Nat Struct Biol. 2001 Aug;8(8):689-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11473259 11473259] | ||
[[Category: Pancreatic elastase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Clifton, I J.]] | [[Category: Clifton, I J.]] | ||
[[Category: Edman, K.]] | [[Category: Edman, K.]] | ||
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[[Category: Wilmouth, R C.]] | [[Category: Wilmouth, R C.]] | ||
[[Category: Wright, P A.]] | [[Category: Wright, P A.]] | ||
[[Category: hydrolase (serine proteinase)]] | [[Category: hydrolase (serine proteinase)]] | ||
[[Category: serine proteinase]] | [[Category: serine proteinase]] | ||
''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 21:01:25 2008'' | ||
Revision as of 21:01, 30 March 2008
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| , resolution 1.7Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Pancreatic elastase, with EC number 3.4.21.36 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SNAPSHOTS OF SERINE PROTEASE CATALYSIS: (B) ACYL-ENZYME INTERMEDIATE BETWEEN PORCINE PANCREATIC ELASTASE AND HUMAN BETA-CASOMORPHIN-7 JUMPED TO PH 10 FOR 10 SECONDS
OverviewOverview
Studies on the catalytic mechanism and inhibition of serine proteases are widely used as paradigms for teaching enzyme catalysis. Ground-breaking work on the structures of chymotrypsin and subtilisin led to the idea of a conserved catalytic triad formed by the active site Ser, His and Asp residues. An oxyanion hole, consisting of the peptide amide of the active site serine and a neighbouring glycine, was identified, and hydrogen bonding in the oxyanion hole was suggested to stabilize the two proposed tetrahedral intermediates on the catalytic pathway. Here we show electron density changes consistent with the formation of a tetrahedral intermediate during the hydrolysis of an acyl-enzyme complex formed between a natural heptapeptide and elastase. No electron density for an enzyme-product complex was observed. The structures also suggest a mechanism for the synchronization of hydrolysis and peptide release triggered by the conversion of the sp2 hybridized carbonyl carbon to an sp3 carbon in the tetrahedral intermediate. This affects the location of the peptide in the active site cleft, triggering the collapse of a hydrogen bonding network between the peptide and the beta-sheet of the active site.
About this StructureAbout this Structure
1HAY is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate., Wilmouth RC, Edman K, Neutze R, Wright PA, Clifton IJ, Schneider TR, Schofield CJ, Hajdu J, Nat Struct Biol. 2001 Aug;8(8):689-94. PMID:11473259
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