1e0k

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{{STRUCTURE_1e0k| PDB=1e0k | SCENE= }}
{{STRUCTURE_1e0k| PDB=1e0k | SCENE= }}
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'''GP4D HELICASE FROM PHAGE T7'''
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===GP4D HELICASE FROM PHAGE T7===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_10892646}}
==About this Structure==
==About this Structure==
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[[Category: Dna replication]]
[[Category: Dna replication]]
[[Category: Helicase]]
[[Category: Helicase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:30:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:56:28 2008''

Revision as of 20:56, 30 June 2008

Image:1e0k.png

Template:STRUCTURE 1e0k

GP4D HELICASE FROM PHAGE T7

Template:ABSTRACT PUBMED 10892646

About this Structure

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

Reference

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

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