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2a8v

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Revision as of 14:37, 17 November 2021

RHO TRANSCRIPTION TERMINATION FACTOR/RNA COMPLEX

Structural highlights

2a8v is a 5 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

The E. coli Rho protein disengages newly transcribed RNA from its DNA template, helping terminate certain transcripts. We have determined the X-ray crystal structure of the RNA-binding domain of Rho complexed to an RNA ligand. Filters that screen both ligand size and chemical functionality line the primary nucleic acid-binding site, imparting sequence specificity to a generic single-stranded nucleic acid-binding fold and explaining the preference of Rho for cytosine-rich RNA. The crystal packing reveals two Rho domain protomers bound to a single RNA with a single base spacer, suggesting that the strong RNA-binding sites of Rho may arise from pairing of RNA-binding modules. Dimerization of symmetric subunits on an asymmetric ligand is developed as a model for allosteric control in the action of the intact Rho hexamer.

The structural basis for terminator recognition by the Rho transcription termination factor.,Bogden CE, Fass D, Bergman N, Nichols MD, Berger JM Mol Cell. 1999 Apr;3(4):487-93. PMID:10230401^[1]

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

References

↑ Bogden CE, Fass D, Bergman N, Nichols MD, Berger JM. The structural basis for terminator recognition by the Rho transcription termination factor. Mol Cell. 1999 Apr;3(4):487-93. PMID:10230401

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2a8v"

@@ Line 3: / Line 3: @@
 <StructureSection load='2a8v' size='340' side='right'caption='[[2a8v]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2a8v]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A8V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A8V FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2a8v]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A8V FirstGlance]. <br>
-</td></tr><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=2a8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a8v OCA], [http://pdbe.org/2a8v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a8v RCSB], [http://www.ebi.ac.uk/pdbsum/2a8v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2a8v ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a8v OCA], [https://pdbe.org/2a8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a8v RCSB], [https://www.ebi.ac.uk/pdbsum/2a8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a8v ProSAT]</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]
+[[https://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]]
@@ Line 30: / Line 30: @@
 ==See Also==
 *[[Helicase 3D structures|Helicase 3D structures]]
-*[[Transcription Termination Factor Rho|Transcription Termination Factor Rho]]
 == References ==
 <references/>

2a8v

From Proteopedia

Revision as of 14:37, 17 November 2021

RHO TRANSCRIPTION TERMINATION FACTOR/RNA COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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