1ofh: Difference between revisions

Revision as of 02:30, 29 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:1ofh.png

Template:STRUCTURE 1ofh

ASYMMETRIC COMPLEX BETWEEN HSLV AND I-DOMAIN DELETED HSLU (H. INFLUENZAE)ASYMMETRIC COMPLEX BETWEEN HSLV AND I-DOMAIN DELETED HSLU (H. INFLUENZAE)

Template:ABSTRACT PUBMED 12823960

About this StructureAbout this Structure

1OFH is a Protein complex structure of sequences from Haemophilus influenzae. Full crystallographic information is available from OCA.

ReferenceReference

Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome., Kwon AR, Kessler BM, Overkleeft HS, McKay DB, J Mol Biol. 2003 Jul 4;330(2):185-95. PMID:12823960

Page seeded by OCA on Tue Jul 29 02:30:02 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1ofh.gif|left|200px]]
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 {{STRUCTURE_1ofh|  PDB=1ofh  |  SCENE=  }}
-'''ASYMMETRIC COMPLEX BETWEEN HSLV AND I-DOMAIN DELETED HSLU (H. INFLUENZAE)'''
+===ASYMMETRIC COMPLEX BETWEEN HSLV AND I-DOMAIN DELETED HSLU (H. INFLUENZAE)===
-==Overview==
+<!--
-In the prokaryotic homolog of the eukaryotic proteasome, HslUV, the "double donut" HslV protease is allosterically activated by HslU, an AAA protein of the Clp/Hsp100 family consisting of three (amino-terminal, carboxy-terminal, and intermediate) domains. The intermediate domains of HslU, which extend like tentacles from the hexameric ring formed by the amino-terminal and carboxy-terminal domains, have been deleted; an asymmetric HslU(DeltaI)(6)HslV(12) complex has been crystallized; and the structure has been solved to 2.5A resolution, revealing an assembly in which a HslU(DeltaI) hexamer binds one end of the HslV dodecamer. The conformation of the protomers of the HslU(DeltaI)-complexed HslV hexamer is similar to that in the symmetric wild-type HslUV complex, while the protomer conformation of the uncomplexed HslV hexamer is similar to that of HslV alone. Reaction in the crystals with a vinyl sulfone inhibitor reveals that the HslU(DeltaI)-complexed HslV hexamer is active, while the uncomplexed HslV hexamer is inactive. These results confirm that HslV can be activated by binding of a hexameric HslU(DeltaI)(6) ring lacking the I domains, that activation is effected through a conformational change in HslV rather than through alteration of the size of the entry channel into the protease catalytic cavity, and that the two HslV(6) rings in the protease dodecamer are activated independently rather than cooperatively.
+The line below this paragraph, {{ABSTRACT_PUBMED_12823960}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12823960 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12823960}}
 ==About this Structure==
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 [[Category: Chaperone]]
 [[Category: Hydrolase]]
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