1npc

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(New page: 200px<br /><applet load="1npc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1npc, resolution 2.0&Aring;" /> '''THE STRUCTURE OF NEUT...)
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[[Image:1npc.jpg|left|200px]]<br /><applet load="1npc" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1npc, resolution 2.0&Aring;" />
caption="1npc, resolution 2.0&Aring;" />
'''THE STRUCTURE OF NEUTRAL PROTEASE FROM BACILLUS CEREUS AT 0.2-NM RESOLUTION'''<br />
'''THE STRUCTURE OF NEUTRAL PROTEASE FROM BACILLUS CEREUS AT 0.2-NM RESOLUTION'''<br />
==Overview==
==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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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==
==About this Structure==
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1NPC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus] with CA and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NPC OCA].
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1NPC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPC OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermolysin]]
[[Category: Thermolysin]]
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[[Category: Jansonius, J.N.]]
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[[Category: Jansonius, J N.]]
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[[Category: Pauptit, R.A.]]
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[[Category: Pauptit, R A.]]
[[Category: Stark, W.]]
[[Category: Stark, W.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: hydrolase(metalloproteinase)]]
[[Category: hydrolase(metalloproteinase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:27:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:33 2008''

Revision as of 12:08, 21 February 2008


1npc, resolution 2.0Å

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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 with and as ligands. Active as Thermolysin, with EC number 3.4.24.27 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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