1g3k: Difference between revisions

Revision as of 04:21, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1g3k.png

Template:STRUCTURE 1g3k

CRYSTAL STRUCTURE OF THE H. INFLUENZAE PROTEASE HSLV AT 1.9 A RESOLUTIONCRYSTAL STRUCTURE OF THE H. INFLUENZAE PROTEASE HSLV AT 1.9 A RESOLUTION

Template:ABSTRACT PUBMED 11106733

About this StructureAbout this Structure

1G3K is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.

ReferenceReference

Crystal and solution structures of an HslUV protease-chaperone complex., Sousa MC, Trame CB, Tsuruta H, Wilbanks SM, Reddy VS, McKay DB, Cell. 2000 Nov 10;103(4):633-43. PMID:11106733

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OCA

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-'''CRYSTAL STRUCTURE OF THE H. INFLUENZAE PROTEASE HSLV AT 1.9 A RESOLUTION'''
+===CRYSTAL STRUCTURE OF THE H. INFLUENZAE PROTEASE HSLV AT 1.9 A RESOLUTION===
-==Overview==
+<!--
-HslUV is a "prokaryotic proteasome" composed of the HslV protease and the HslU ATPase, a chaperone of the Clp/Hsp100 family. The 3.4 A crystal structure of an HslUV complex is presented here. Two hexameric ATP binding rings of HslU bind intimately to opposite sides of the HslV protease; the HslU "intermediate domains" extend outward from the complex. The solution structure of HslUV, derived from small angle X-ray scattering data under conditions where the complex is assembled and active, agrees with this crystallographic structure. When the complex forms, the carboxy-terminal helices of HslU distend and bind between subunits of HslV, and the apical helices of HslV shift substantially, transmitting a conformational change to the active site region of the protease.
+The line below this paragraph, {{ABSTRACT_PUBMED_11106733}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11106733}}
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 [[Category: Hydrolase]]
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