1e0k: Difference between revisions
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[[Image:1e0k.jpg|left|200px]] | [[Image:1e0k.jpg|left|200px]] | ||
'''GP4D HELICASE FROM PHAGE T7''' | {{Structure | ||
|PDB= 1e0k |SIZE=350|CAPTION= <scene name='initialview01'>1e0k</scene>, resolution 3.30Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= GENE 4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Bacteriophage T7]) | |||
}} | |||
'''GP4D HELICASE FROM PHAGE T7''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E0K is a [ | 1E0K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t7 Bacteriophage t7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0K OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10892646 10892646] | ||
[[Category: Bacteriophage t7]] | [[Category: Bacteriophage t7]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: helicase]] | [[Category: helicase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:47:31 2008'' | ||
Revision as of 11:47, 20 March 2008
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| , resolution 3.30Å | |||||||
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| Gene: | GENE 4 (Bacteriophage T7) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GP4D HELICASE FROM PHAGE T7
OverviewOverview
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 StructureAbout this Structure
1E0K is a Single protein structure of sequence from Bacteriophage 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
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