1e0k: Difference between revisions

Revision as of 23:56, 30 June 2008

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File:1e0k.png

Template:STRUCTURE 1e0k

GP4D HELICASE FROM PHAGE T7GP4D HELICASE FROM PHAGE T7

Template:ABSTRACT PUBMED 10892646

About this StructureAbout this Structure

1E0K is a Single protein structure of sequence from Enterobacteria phage t7. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides., Singleton MR, Sawaya MR, Ellenberger T, Wigley DB, Cell. 2000 Jun 9;101(6):589-600. PMID:10892646

Page seeded by OCA on Mon Jun 30 23:56:28 2008

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

OCA

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-'''GP4D HELICASE FROM PHAGE T7'''
+===GP4D HELICASE FROM PHAGE T7===
-==Overview==
+<!--
-We have determined the crystal structure of an active, hexameric fragment of the gene 4 helicase from bacteriophage T7. The structure reveals how subunit contacts stabilize the hexamer. Deviation from expected six-fold symmetry of the hexamer indicates that the structure is of an intermediate on the catalytic pathway. The structural consequences of the asymmetry suggest a "binding change" mechanism to explain how cooperative binding and hydrolysis of nucleotides are coupled to conformational changes in the ring that most likely accompany duplex unwinding. The structure of a complex with a nonhydrolyzable ATP analog provides additional evidence for this hypothesis, with only four of the six possible nucleotide binding sites being occupied in this conformation of the hexamer. This model suggests a mechanism for DNA translocation.
+The line below this paragraph, {{ABSTRACT_PUBMED_10892646}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10892646 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10892646}}
 ==About this Structure==
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 [[Category: Dna replication]]
 [[Category: Helicase]]
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