1npc

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{{STRUCTURE_1npc| PDB=1npc | SCENE= }}
{{STRUCTURE_1npc| PDB=1npc | SCENE= }}
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'''THE STRUCTURE OF NEUTRAL PROTEASE FROM BACILLUS CEREUS AT 0.2-NM RESOLUTION'''
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===THE STRUCTURE OF NEUTRAL PROTEASE FROM BACILLUS CEREUS AT 0.2-NM RESOLUTION===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 1633827 is the PubMed ID number.
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{{ABSTRACT_PUBMED_1633827}}
==About this Structure==
==About this Structure==
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[[Category: Pauptit, R A.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:20:07 2008''

Revision as of 17:20, 28 July 2008

Image:1npc.png

Template:STRUCTURE 1npc

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

Template:ABSTRACT PUBMED 1633827

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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