1sat
From Proteopedia
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'''CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS''' | '''CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Baumann, U.]] | [[Category: Baumann, U.]] | ||
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| - | [[Category: | + | [[Category: Parallel beta roll]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:29:31 2008'' | |
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Revision as of 05:29, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 08:29:31 2008
