1hb0: Difference between revisions

Revision as of 07:55, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1hb0.png

Template:STRUCTURE 1hb0

SNAPSHOTS OF SERINE PROTEASE CATALYSIS: (D) ACYL-ENZYME INTERMEDIATE BETWEEN PORCINE PANCREATIC ELASTASE AND HUMAN BETA-CASOMORPHIN-7 JUMPED TO PH 10 FOR 2 MINUTESSNAPSHOTS OF SERINE PROTEASE CATALYSIS: (D) ACYL-ENZYME INTERMEDIATE BETWEEN PORCINE PANCREATIC ELASTASE AND HUMAN BETA-CASOMORPHIN-7 JUMPED TO PH 10 FOR 2 MINUTES

Template:ABSTRACT PUBMED 11473259

About this StructureAbout this Structure

1HB0 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

Page seeded by OCA on Tue Jul 1 07:55:18 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1hb0|  PDB=1hb0  |  SCENE=  }}
-'''SNAPSHOTS OF SERINE PROTEASE CATALYSIS: (D) ACYL-ENZYME INTERMEDIATE BETWEEN PORCINE PANCREATIC ELASTASE AND HUMAN BETA-CASOMORPHIN-7 JUMPED TO PH 10 FOR 2 MINUTES'''
+===SNAPSHOTS OF SERINE PROTEASE CATALYSIS: (D) ACYL-ENZYME INTERMEDIATE BETWEEN PORCINE PANCREATIC ELASTASE AND HUMAN BETA-CASOMORPHIN-7 JUMPED TO PH 10 FOR 2 MINUTES===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11473259}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11473259 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11473259}}
 ==About this Structure==
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 [[Category: Wright, P A.]]
 [[Category: Serine proteinase]]
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