2ht1: Difference between revisions
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[[Image:2ht1.gif|left|200px]] | [[Image:2ht1.gif|left|200px]] | ||
'''The closed ring structure of the Rho transcription termination factor in complex with nucleic acid in the motor domains''' | {{Structure | ||
|PDB= 2ht1 |SIZE=350|CAPTION= <scene name='initialview01'>2ht1</scene>, resolution 3.51Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= rho, nitA, psuA, rnsC, sbaA, tsu ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''The closed ring structure of the Rho transcription termination factor in complex with nucleic acid in the motor domains''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2HT1 is a [ | 2HT1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HT1 OCA]. | ||
==Reference== | ==Reference== | ||
Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor., Skordalakes E, Berger JM, Cell. 2006 Nov 3;127(3):553-64. PMID:[http:// | Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor., Skordalakes E, Berger JM, Cell. 2006 Nov 3;127(3):553-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17081977 17081977] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: translocase]] | [[Category: translocase]] | ||
''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 17:21:14 2008'' | ||
Revision as of 18:21, 20 March 2008
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| , resolution 3.51Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | rho, nitA, psuA, rnsC, sbaA, tsu (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The closed ring structure of the Rho transcription termination factor in complex with nucleic acid in the motor domains
OverviewOverview
Hexameric helicases and translocases are required for numerous essential nucleic-acid transactions. To better understand the mechanisms by which these enzymes recognize target substrates and use nucleotide hydrolysis to power molecular movement, we have determined the structure of the Rho transcription termination factor, a hexameric RNA/DNA helicase, with single-stranded RNA bound to the motor domains of the protein. The structure reveals a closed-ring "trimer of dimers" conformation for the hexamer that contains an unanticipated arrangement of conserved loops required for nucleic-acid translocation. RNA extends across a shallow intersubunit channel formed by conserved amino acids required for RNA-stimulated ATP hydrolysis and translocation and directly contacts a conserved lysine, just upstream of the catalytic GKT triad, in the phosphate-binding (P loop) motif of the ATP-binding pocket. The structure explains the molecular effects of numerous mutations and provides new insights into the links between substrate recognition, ATP turnover, and coordinated strand movement.
About this StructureAbout this Structure
2HT1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor., Skordalakes E, Berger JM, Cell. 2006 Nov 3;127(3):553-64. PMID:17081977
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