2o8l
From Proteopedia
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(New page: 200px<br /><applet load="2o8l" size="350" color="white" frame="true" align="right" spinBox="true" caption="2o8l, resolution 1.50Å" /> '''Structure of V8 prot...)
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Revision as of 19:07, 29 January 2008
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Structure of V8 protease from staphylococcus aureus
Overview
V8 protease, an extracellular protease of Staphylococcus aureus, is, related to the pancreatic serine proteases. The enzyme cleaves peptide, bonds exclusively on the carbonyl side of aspartate and glutamate, residues. Unlike the pancreatic serine proteases, V8 protease possesses no, disulfide bridges. This is a major evolutionary difference, as all, pancreatic proteases have at least two disulfide bridges. The structure of, V8 protease shows structural similarity with several other serine, proteases, specifically the epidermolytic toxins A and B from S. aureus, and trypsin, in which the conformation of the active site is almost, identical. V8 protease is also unique in that the positively charged, N-terminus is involved in determining the substrate-specificity of the, enzyme.
About this Structure
2O8L is a Single protein structure of sequence from Staphylococcus aureus with as ligand. Active as Glutamyl endopeptidase, with EC number 3.4.21.19 Full crystallographic information is available from OCA.
Reference
The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus., Prasad L, Leduc Y, Hayakawa K, Delbaere LT, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):256-9. Epub 2004, Jan 23. PMID:14747701
Page seeded by OCA on Tue Jan 29 21:07:08 2008
