1NPC

THE STRUCTURE OF NEUTRAL PROTEASE FROM BACILLUS CEREUS AT 0.2-NM RESOLUTION

Summary for 1NPC

• Entry DOI: 10.2210/pdb1npc/pdb
• Descriptor: NEUTRAL PROTEASE, CALCIUM ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: hydrolase(metalloproteinase)
• Biological source: Bacillus cereus
• Cellular location: Secreted: P05806
• Total number of polymer chains: 1
• Total formula weight: 34042.22

Authors

Stark, W.,Pauptit, R.A.,Jansonius, J.N. (deposition date: 1992-01-08, release date: 1993-10-31, Last modification date: 2024-02-14)

Primary citation

Stark, W.,Pauptit, R.A.,Wilson, K.S.,Jansonius, J.N.
The structure of neutral protease from Bacillus cereus at 0.2-nm resolution.
Eur.J.Biochem., 207:781-791, 1992

PubMed Abstract: 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.

PubMed: 1633827
DOI: 10.1111/j.1432-1033.1992.tb17109.x

Experimental method

X-RAY DIFFRACTION (2 Å)