5tbz

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Revision as of 19:02, 15 November 2017

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E. Coli RNA Polymerase complexed with NusG

Structural highlights

5tbz is a 10 chain structure with sequence from Eco45 and Eco57. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	rpoA, Z4665, ECs4160 (ECO57), rpoB, ECS88_4448 (ECO45), rpoC, Z5561, ECs4911 (ECO57), nusG, Z5555, ECs4905 (ECO57)
Activity:	DNA-directed RNA polymerase, with EC number 2.7.7.6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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Function

[NUSG_ECO57] Participates in transcription elongation, termination and antitermination. In the absence of Rho, increases the rate of transcription elongation by the RNA polymerase (RNAP), probably by partially suppressing pausing. In the presence of Rho, modulates most Rho-dependent termination events by interacting with the RNAP to render the complex more susceptible to the termination activity of Rho. May be required to overcome a kinetic limitation of Rho to function at certain terminators. Also involved in ribosomal RNA transcriptional antitermination.[HAMAP-Rule:MF_00948] [RPOA_ECO57] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [RPOC_ECO57] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [RPOB_ECO45] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

Publication Abstract from PubMed

NusG is an essential transcription factor that plays multiple key regulatory roles in transcription elongation, termination and coupling translation and transcription. The core role of NusG is to enhance transcription elongation and RNA polymerase processivity. Here, we present the structure of Escherichia coli RNA polymerase complexed with NusG. The structure shows that the NusG N-terminal domain (NGN) binds at the central cleft of RNA polymerase surrounded by the beta' clamp helices, the beta protrusion, and the beta lobe domains to close the promoter DNA binding channel and constrain the beta' clamp domain, but with an orientation that is different from the one observed in the archaeal beta' clamp-Spt4/5 complex. The structure also allows us to construct a reliable model of the complete NusG-associated transcription elongation complex, suggesting that the NGN domain binds at the upstream fork junction of the transcription elongation complex, similar to sigma2 in the transcription initiation complex, to stabilize the junction, and therefore enhances transcription processivity.

Structural insights into NusG regulating transcription elongation.,Liu B, Steitz TA Nucleic Acids Res. 2016 Nov 29. pii: gkw1159. PMID:27899640^[1]

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

References

↑ Liu B, Steitz TA. Structural insights into NusG regulating transcription elongation. Nucleic Acids Res. 2016 Nov 29. pii: gkw1159. PMID:27899640 doi:http://dx.doi.org/10.1093/nar/gkw1159

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5tbz"

@@ Line 3: / Line 3: @@
 <StructureSection load='5tbz' size='340' side='right' caption='[[5tbz]], [[Resolution|resolution]] 7.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5tbz]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TBZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TBZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5tbz]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco45 Eco45] and [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TBZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TBZ FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] </span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpoA, Z4665, ECs4160 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57]), rpoB, ECS88_4448 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=585035 ECO45]), rpoC, Z5561, ECs4911 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57]), nusG, Z5555, ECs4905 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] </span></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=5tbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tbz OCA], [http://pdbe.org/5tbz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tbz RCSB], [http://www.ebi.ac.uk/pdbsum/5tbz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tbz ProSAT]</span></td></tr>
 </table>
@@ Line 24: / Line 25: @@
 </StructureSection>
 [[Category: DNA-directed RNA polymerase]]
+[[Category: Eco45]]
+[[Category: Eco57]]
 [[Category: Liu, B]]
 [[Category: Steitz, T A]]

5tbz

From Proteopedia

Revision as of 19:02, 15 November 2017

E. Coli RNA Polymerase complexed with NusG

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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