Structural highlights
Function
[NPRE_BACCE] Extracellular zinc metalloprotease.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of the neutral protease from Bacillus cereus has been refined to an R factor of 17.5% at 0.2-nm resolution. The enzyme, an extracellular metalloendopeptidase, consists of two domains and binds one zinc and four calcium ions. The structure is very similar to that of thermolysin, with which the enzyme shares 73% amino-acid sequence identity. The active-site cleft between the two domains is wider in neutral protease than in thermolysin. This suggests the presence of a flexible hinge region between the two domains, which may assist enzyme action. The high-resolution analysis allows detailed examination of possible causes for the difference in thermostability between neutral protease and thermolysin.
The structure of neutral protease from Bacillus cereus at 0.2-nm resolution.,Stark W, Pauptit RA, Wilson KS, Jansonius JN Eur J Biochem. 1992 Jul 15;207(2):781-91. PMID:1633827[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stark W, Pauptit RA, Wilson KS, Jansonius JN. The structure of neutral protease from Bacillus cereus at 0.2-nm resolution. Eur J Biochem. 1992 Jul 15;207(2):781-91. PMID:1633827
