2agi
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(New page: 200px<br /><applet load="2agi" size="450" color="white" frame="true" align="right" spinBox="true" caption="2agi, resolution 1.140Å" /> '''The leupeptin-tryps...)
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Revision as of 05:59, 21 November 2007
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The leupeptin-trypsin covalent complex at 1.14 A resolution
Overview
Atomic resolution structures of trypsin acyl-enzymes and a tetrahedral, intermediate analog, along with previously solved structures representing, the Michaelis complex, are used to reconstruct events in the catalytic, cycle of this classic serine protease. Structural comparisons provide, insight into active site adjustments involved in catalysis. Subtle motions, of the catalytic serine and histidine residues coordinated with, translation of the substrate reaction center are seen to favor the forward, progress of the acylation reaction. The structures also clarify the attack, trajectory of the hydrolytic water in the deacylation reaction.
About this Structure
2AGI is a Single protein structure of sequence from Bos taurus with SO4, CA and ACE as ligands. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates., Radisky ES, Lee JM, Lu CJ, Koshland DE Jr, Proc Natl Acad Sci U S A. 2006 May 2;103(18):6835-40. Epub 2006 Apr 24. PMID:16636277
Page seeded by OCA on Wed Nov 21 08:06:26 2007
