1SAT

CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS

Summary for 1SAT

• Entry DOI: 10.2210/pdb1sat/pdb
• Descriptor: SERRATIA PROTEASE, ZINC ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: parallel beta helix, parallel beta roll, hydrolase (serine protease)
• Biological source: Serratia marcescens
• Cellular location: Secreted: P23694
• Total number of polymer chains: 1
• Total formula weight: 50659.04

Authors

Baumann, U. (deposition date: 1994-07-04, release date: 1995-07-31, Last modification date: 2024-02-14)

Primary citation

Baumann, U.
Crystal structure of the 50 kDa metallo protease from Serratia marcescens.
J.Mol.Biol., 242:244-251, 1994

PubMed Abstract: 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.

PubMed: 8089845
DOI: 10.1006/jmbi.1994.1576

Experimental method

X-RAY DIFFRACTION (1.75 Å)