1sat
From Proteopedia
|
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 and 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
Page seeded by OCA on Thu Feb 21 14:59:36 2008
