1a63
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a63 OCA], [http://www.ebi.ac.uk/pdbsum/1a63 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a63 RCSB]</span> | ||
}} | }} | ||
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[[Category: transcription termination]] | [[Category: transcription termination]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:34:04 2008'' |
Revision as of 15:34, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE NMR STRUCTURE OF THE RNA BINDING DOMAIN OF E.COLI RHO FACTOR SUGGESTS POSSIBLE RNA-PROTEIN INTERACTIONS, 10 STRUCTURES
Overview
Rho protein is an essential hexameric RNA-DNA helicase that binds nascent mRNA transcripts and terminates transcription in a wide variety of eubacterial species. The NMR solution structure of the RNA binding domain of rho, rho130, is presented. This structure consists of two sub-domains, an N-terminal three-helix bundle and a C-terminal beta-barrel that is structurally similar to the oligosaccharide/oligonucleotide binding (OB) fold. Chemical shift changes of rho130 upon RNA binding and previous mutagenetic analyses of intact rho suggest that residues Asp 60, Phe 62, Phe 64, and Arg 66 are critical for binding and support the hypothesis that ssRNA/ssDNA binding is localized in the beta-barrel sub-domain. On the basis of these studies and the tertiary structure of rho130, we propose that residues Asp 60, Phe 62, Phe 64, Arg 66, Tyr 80, Lys 105, and Arg 109 participate in RNA-protein interactions.
About this Structure
1A63 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions., Briercheck DM, Wood TC, Allison TJ, Richardson JP, Rule GS, Nat Struct Biol. 1998 May;5(5):393-9. PMID:9587002
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