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PDBsum entry 1a62
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Transcription termination
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PDB id
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1a62
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the RNA-Binding domain from transcription termination factor rho.
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Authors
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T.J.Allison,
T.C.Wood,
D.M.Briercheck,
F.Rastinejad,
J.P.Richardson,
G.S.Rule.
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Ref.
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Nat Struct Biol, 1998,
5,
352-356.
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PubMed id
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Abstract
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Transcription termination factor rho is an ATP-dependent hexameric helicase
found in most eubacterial species. The Escherichia coli rho monomer consists of
two domains, an RNA-binding domain (residues 1-130) and an ATPase domain
(residues 131-419). The ATPase domain is homologous to the beta subunit of
F1-ATPase. Here, we report that the crystal structure of the RNA-binding domain
of rho (rho130) at 1.55 A confirms that rho130 contains the
oligosaccharide/oligonucleotide-binding (OB) fold, a five stranded beta-barrel.
The beta-barrel of rho130 is also surprisingly similar to the N-terminal
beta-barrel of F1 ATPase, extending the applicability of F1 ATPase as a
structural model for hexameric rho.
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Secondary reference #1
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Title
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The nmr structure of the RNA binding domain of e. Coli rho factor suggests possible RNA-Protein interactions.
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Authors
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D.M.Briercheck,
T.C.Wood,
T.J.Allison,
J.P.Richardson,
G.S.Rule.
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Ref.
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Nat Struct Biol, 1998,
5,
393-399.
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PubMed id
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Secondary reference #2
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Title
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1h, 15n and 13c resonance assignments and secondary structure determination of the RNA-Binding domain of e.Coli rho protein.
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Authors
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D.M.Briercheck,
T.J.Allison,
J.P.Richardson,
J.F.Ellena,
T.C.Wood,
G.S.Rule.
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Ref.
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J Biomol Nmr, 1996,
8,
429-444.
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PubMed id
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