1sat
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(New page: 200px<br /><applet load="1sat" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sat, resolution 1.75Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 00:06, 21 November 2007
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CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS
Overview
The crystal structure of the 50 kDa metalloprotease from the Gram-negative, bacterium Serratia marcescens has been solved and refined to a, crystallographic R-factor of 0.192 at 1.80 A resolution. The structure is, very similar to that of alkaline protease from Pseudomonas aeruginosa, in, particular the calcium binding "parallel beta roll" motif is completely, conserved. The N-terminal proteolytic domain shows the typical "metzincin", fold. The active sites of the two enzymes are slightly different, Tyr216, is a Zn ligand in the Serratia metallo protease. The loops 70-77 and, 122-132, which encompass the active site cleft, differ due to insertions, and deletions so that the Serratia metallo protease seems to have a more, open site than the alkaline protease.
About this Structure
1SAT is a Single protein structure of sequence from Serratia marcescens with ZN and CA as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the 50 kDa metallo protease from Serratia marcescens., Baumann U, J Mol Biol. 1994 Sep 23;242(3):244-51. PMID:8089845
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