4xwj: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4xwj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XWJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[4xwj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XWJ 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=4xwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xwj OCA], [https://pdbe.org/4xwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xwj RCSB], [https://www.ebi.ac.uk/pdbsum/4xwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xwj ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.095&#8491;</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=4xwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xwj OCA], [https://pdbe.org/4xwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xwj RCSB], [https://www.ebi.ac.uk/pdbsum/4xwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xwj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/RSD_ECOLI RSD_ECOLI] Binds RpoD and negatively regulates RpoD-mediated transcription activation by preventing the interaction between the primary sigma factor RpoD with the catalytic core of the RNA polymerase and with promoter DNA. May be involved in replacement of the RNA polymerase sigma subunit from RpoD to RpoS during the transition from exponential growth to the stationary phase.<ref>PMID:9560209</ref> <ref>PMID:10368152</ref>  
[https://www.uniprot.org/uniprot/RSD_ECOLI RSD_ECOLI] Binds RpoD and negatively regulates RpoD-mediated transcription activation by preventing the interaction between the primary sigma factor RpoD with the catalytic core of the RNA polymerase and with promoter DNA. May be involved in replacement of the RNA polymerase sigma subunit from RpoD to RpoS during the transition from exponential growth to the stationary phase.<ref>PMID:9560209</ref> <ref>PMID:10368152</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Histidine-containing phosphocarrier protein (HPr) is a general component of the bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) involved in the phosphorylation-coupled transport of numerous sugars called PTS sugars. HPr mainly exists in a dephosphorylated form in the presence of PTS sugars in the medium, while its phosphorylation increases in the absence of PTS sugars. A recent study revealed that the dephosphorylated form of HPr binds and antagonizes the function of the antisigma factor Rsd. This anti-sigma factor sequesters the housekeeping sigma factor sigma(70) to facilitate switching of the sigma subunit on RNA polymerase from sigma(70) to the stress-responsive sigma factor sigma(S) in stationary-phase cells. In this study, the structure of the complex of Rsd and HPr was determined at 2.1 A resolution and revealed that the binding site for HPr on the surface of Rsd partly overlaps with that for sigma(70). The localization of the phosphorylation site on HPr at the binding interface for Rsd explains why phosphorylation of HPr abolishes its binding to Rsd. The mutation of crucial residues involved in the HPr-Rsd interaction significantly influenced the competition between HPr and sigma(70) for binding to Rsd both in vitro and in vivo. The results provide a structural basis for the linkage of global gene regulation to nutrient availability in the external environment.
Structural basis for the sequestration of the anti-sigma(70) factor Rsd from sigma(70) by the histidine-containing phosphocarrier protein HPr.,Park YH, Um SH, Song S, Seok YJ, Ha NC Acta Crystallogr D Biol Crystallogr. 2015 Oct;71(Pt 10):1998-2008. doi:, 10.1107/S1399004715013759. Epub 2015 Sep 26. PMID:26457424<ref>PMID:26457424</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4xwj" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Latest revision as of 12:02, 20 March 2024

Histidine-containing phosphocarrier protein (HPr) and antisigma factor Rsd complexHistidine-containing phosphocarrier protein (HPr) and antisigma factor Rsd complex

Structural highlights

4xwj is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.095Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RSD_ECOLI Binds RpoD and negatively regulates RpoD-mediated transcription activation by preventing the interaction between the primary sigma factor RpoD with the catalytic core of the RNA polymerase and with promoter DNA. May be involved in replacement of the RNA polymerase sigma subunit from RpoD to RpoS during the transition from exponential growth to the stationary phase.[1] [2]

See Also

References

  1. ↑ Jishage M, Ishihama A. A stationary phase protein in Escherichia coli with binding activity to the major sigma subunit of RNA polymerase. Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):4953-8. PMID:9560209
  2. ↑ Jishage M, Ishihama A. Transcriptional organization and in vivo role of the Escherichia coli rsd gene, encoding the regulator of RNA polymerase sigma D. J Bacteriol. 1999 Jun;181(12):3768-76. PMID:10368152

4xwj, resolution 2.10Å

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