1npc | pdb_00001npc
THE STRUCTURE OF NEUTRAL PROTEASE FROM BACILLUS CEREUS AT 0.2-NM RESOLUTION
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| 1npc, resolution 2.0Å | |||||||||||||
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| Ligands: | CA, ZN | ||||||||||||
| Activity: | Thermolysin, with EC number 3.4.24.27 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
1NPC is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.
Reference
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
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