1e0k
From Proteopedia
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'''GP4D HELICASE FROM PHAGE T7''' | '''GP4D HELICASE FROM PHAGE T7''' | ||
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[[Category: Singleton, M R.]] | [[Category: Singleton, M R.]] | ||
[[Category: Wigley, D B.]] | [[Category: Wigley, D B.]] | ||
| - | [[Category: | + | [[Category: Atpase]] |
| - | [[Category: | + | [[Category: Dna replication]] |
| - | [[Category: | + | [[Category: Helicase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:30:39 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 11:30, 2 May 2008
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.
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 Page seeded by OCA on Fri May 2 14:30:39 2008
