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< | ==Solution structure of Gp2== | ||
<StructureSection load='2wnm' size='340' side='right'caption='[[2wnm]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wnm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpt7 Bpt7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WNM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WNM FirstGlance]. <br> | |||
</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=2wnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wnm OCA], [https://pdbe.org/2wnm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wnm RCSB], [https://www.ebi.ac.uk/pdbsum/2wnm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wnm ProSAT]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wn/2wnm_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2wnm ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Infection of Escherichia coli by the T7 phage leads to rapid and selective inhibition of the host RNA polymerase (RNAP)-a multi-subunit enzyme responsible for gene transcription-by a small ( approximately 7 kDa) phage-encoded protein called Gp2. Gp2 is also a potent inhibitor of E. coli RNAP in vitro. Here we describe the first atomic resolution structure of Gp2, which reveals a distinct run of surface-exposed negatively charged amino acid residues on one side of the molecule. Our comprehensive mutagenesis data reveal that two conserved arginine residues located on the opposite side of Gp2 are important for binding to and inhibition of RNAP. Based on a structural model of the Gp2-RNAP complex, we propose that inhibition of transcription by Gp2 involves prevention of RNAP-promoter DNA interactions required for stable DNA strand separation and maintenance of the "transcription bubble" near the transcription start site, an obligatory step in the formation of a transcriptionally competent promoter complex. | |||
T7 phage protein Gp2 inhibits the Escherichia coli RNA polymerase by antagonizing stable DNA strand separation near the transcription start site.,Camara B, Liu M, Reynolds J, Shadrin A, Liu B, Kwok K, Simpson P, Weinzierl R, Severinov K, Cota E, Matthews S, Wigneshweraraj SR Proc Natl Acad Sci U S A. 2010 Feb 2;107(5):2247-52. Epub 2010 Jan 19. PMID:20133868<ref>PMID:20133868</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2wnm" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Bpt7]] | ||
[[Category: Large Structures]] | |||
[[Category: Camara, B]] | |||
== | [[Category: Cota, E]] | ||
< | [[Category: Liu, B]] | ||
[[Category: | [[Category: Liu, M]] | ||
[[Category: Camara, B | [[Category: Matthews, S]] | ||
[[Category: Cota, E | [[Category: Severinovc, K]] | ||
[[Category: Liu, B | [[Category: Shadrinc, A]] | ||
[[Category: Liu, M | [[Category: Simpson, P]] | ||
[[Category: Matthews, S | [[Category: Weinzierl, R]] | ||
[[Category: Severinovc, K | [[Category: Wigneshweraraj, S R]] | ||
[[Category: Shadrinc, A | |||
[[Category: Simpson, P | |||
[[Category: Weinzierl, R | |||
[[Category: Wigneshweraraj, S R | |||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Small protein inhibntor bacterial rna polymerase]] | [[Category: Small protein inhibntor bacterial rna polymerase]] | ||
Latest revision as of 14:11, 6 April 2022
Solution structure of Gp2Solution structure of Gp2
Structural highlights
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 PubMedInfection of Escherichia coli by the T7 phage leads to rapid and selective inhibition of the host RNA polymerase (RNAP)-a multi-subunit enzyme responsible for gene transcription-by a small ( approximately 7 kDa) phage-encoded protein called Gp2. Gp2 is also a potent inhibitor of E. coli RNAP in vitro. Here we describe the first atomic resolution structure of Gp2, which reveals a distinct run of surface-exposed negatively charged amino acid residues on one side of the molecule. Our comprehensive mutagenesis data reveal that two conserved arginine residues located on the opposite side of Gp2 are important for binding to and inhibition of RNAP. Based on a structural model of the Gp2-RNAP complex, we propose that inhibition of transcription by Gp2 involves prevention of RNAP-promoter DNA interactions required for stable DNA strand separation and maintenance of the "transcription bubble" near the transcription start site, an obligatory step in the formation of a transcriptionally competent promoter complex. T7 phage protein Gp2 inhibits the Escherichia coli RNA polymerase by antagonizing stable DNA strand separation near the transcription start site.,Camara B, Liu M, Reynolds J, Shadrin A, Liu B, Kwok K, Simpson P, Weinzierl R, Severinov K, Cota E, Matthews S, Wigneshweraraj SR Proc Natl Acad Sci U S A. 2010 Feb 2;107(5):2247-52. Epub 2010 Jan 19. PMID:20133868[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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