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1a62

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Revision as of 05:30, 25 December 2014

CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE TRANSCRIPTIONAL TERMINATOR PROTEIN RHO

Structural highlights

1a62 is a 1 chain structure with sequence from Escherichia coli bl21(de3). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[RHO_ECOLI] Facilitates transcription termination by a mechanism that involves rho binding to the nascent RNA, activation of rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. RNA-dependent NTPAse which utilizes all four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01884]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Crystal structure of the RNA-binding domain from transcription termination factor rho.,Allison TJ, Wood TC, Briercheck DM, Rastinejad F, Richardson JP, Rule GS Nat Struct Biol. 1998 May;5(5):352-6. PMID:9586995^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Allison TJ, Wood TC, Briercheck DM, Rastinejad F, Richardson JP, Rule GS. Crystal structure of the RNA-binding domain from transcription termination factor rho. Nat Struct Biol. 1998 May;5(5):352-6. PMID:9586995

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a62"

@@ Line 6: / Line 6: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a62 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a62 RCSB], [http://www.ebi.ac.uk/pdbsum/1a62 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/RHO_ECOLI RHO_ECOLI]] Facilitates transcription termination by a mechanism that involves rho binding to the nascent RNA, activation of rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. RNA-dependent NTPAse which utilizes all four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01884]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1a62

From Proteopedia

Revision as of 05:30, 25 December 2014

CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE TRANSCRIPTIONAL TERMINATOR PROTEIN RHO

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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