1npc

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[[Image:1npc.jpg|left|200px]]
[[Image:1npc.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1npc |SIZE=350|CAPTION= <scene name='initialview01'>1npc</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1npc", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1npc| PDB=1npc | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1npc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1npc OCA], [http://www.ebi.ac.uk/pdbsum/1npc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1npc RCSB]</span>
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}}
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'''THE STRUCTURE OF NEUTRAL PROTEASE FROM BACILLUS CEREUS AT 0.2-NM RESOLUTION'''
'''THE STRUCTURE OF NEUTRAL PROTEASE FROM BACILLUS CEREUS AT 0.2-NM RESOLUTION'''
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[[Category: Pauptit, R A.]]
[[Category: Pauptit, R A.]]
[[Category: Stark, W.]]
[[Category: Stark, W.]]
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[[Category: hydrolase(metalloproteinase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:48:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:33:35 2008''
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Revision as of 23:48, 2 May 2008

Image:1npc.jpg

Template:STRUCTURE 1npc

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


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 Page seeded by OCA on Sat May 3 02:48:54 2008

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