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4llg

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Revision as of 20:53, 5 August 2016

Crystal Structure Analysis of the E.coli holoenzyme/Gp2 complex

Structural highlights

4llg is a 14 chain structure with sequence from Bpt7, Ecobw, Ecod1 and Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4ljz, 4lk0, 4lk1
Gene:	rpoA, EcDH1_0418, ECDH1ME8569_3173 (ECOD1), rpoB, EcDH1_4008, ECDH1ME8569_3846 (ECOD1), rpoC, BWG_3647 (ECOBW), rpoZ, EcDH1_0056, ECDH1ME8569_3534 (ECOD1), rpoD, alt, b3067, JW3039 (ECOLI), 2 (BPT7)
Activity:	DNA-directed RNA polymerase, with EC number 2.7.7.6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VRPI_BPT7] Bacterial RNA polymerase inhibitor, which is expressed in the late stage of lytic development, is also essential for continuous synthesis of phage DNA and functions in the packaging of the viral genome into the mature phage particle. [C9QUL2_ECOD1] Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity).[HAMAP-Rule:MF_00366][SAAS:SAAS012293_004_017283] [C9QXI7_ECOD1] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_00059] [C5A0S8_ECOBW] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[SAAS:SAAS012754_004_011999] [C9QV90_ECOD1] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_01321][RuleBase:RU000432] [RPOD_ECOLI] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This is the primary sigma factor of this bacterium.

Publication Abstract from PubMed

Bacteriophage T7 encodes an essential inhibitor of the Escherichia coli host RNA polymerase (RNAP), the product of gene 2 (Gp2). We determined a series of X-ray crystal structures of E. coli RNAP holoenzyme with or without Gp2. The results define the structure and location of the RNAP sigma70 subunit domain 1.1 inside the RNAP active site channel, where it must be displaced by the DNA upon formation of the open promoter complex. The structures and associated data, combined with previous results, allow for a complete delineation of the mechanism for Gp2 inhibition of E. coli RNAP. In the primary inhibition mechanism, Gp2 forms a protein-protein interaction with , preventing the normal egress of from the RNAP active site channel. Gp2 thus misappropriates a domain of the RNAP holoenzyme, , to inhibit the function of the enzyme.

Phage T7 Gp2 inhibition of Escherichia coli RNA polymerase involves misappropriation of sigma70 domain 1.1.,Bae B, Davis E, Brown D, Campbell EA, Wigneshweraraj S, Darst SA Proc Natl Acad Sci U S A. 2013 Nov 11. PMID:24218560^[1]

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

References

↑ Bae B, Davis E, Brown D, Campbell EA, Wigneshweraraj S, Darst SA. Phage T7 Gp2 inhibition of Escherichia coli RNA polymerase involves misappropriation of sigma70 domain 1.1. Proc Natl Acad Sci U S A. 2013 Nov 11. PMID:24218560 doi:http://dx.doi.org/10.1073/pnas.1314576110

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4llg"

@@ Line 1: / Line 1: @@
 ==Crystal Structure Analysis of the E.coli holoenzyme/Gp2 complex==
 <StructureSection load='4llg' size='340' side='right' caption='[[4llg]], [[Resolution|resolution]] 3.79&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpoA, EcDH1_0418, ECDH1ME8569_3173 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=536056 ECOD1]), rpoB, EcDH1_4008, ECDH1ME8569_3846 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=536056 ECOD1]), rpoC, BWG_3647 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=595496 ECOBW]), rpoZ, EcDH1_0056, ECDH1ME8569_3534 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=536056 ECOD1]), rpoD, alt, b3067, JW3039 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), 2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10760 BPT7])</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=4llg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4llg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4llg RCSB], [http://www.ebi.ac.uk/pdbsum/4llg PDBsum]</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=4llg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4llg OCA], [http://pdbe.org/4llg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4llg RCSB], [http://www.ebi.ac.uk/pdbsum/4llg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4llg ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4llg" style="background-color:#fffaf0;"></div>
 ==See Also==

4llg

From Proteopedia

Revision as of 20:53, 5 August 2016

Crystal Structure Analysis of the E.coli holoenzyme/Gp2 complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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