2z2s

From Proteopedia

(Difference between revisions)

Revision as of 04:48, 5 August 2016

Crystal Structure of Rhodobacter sphaeroides SigE in complex with the anti-sigma ChrR

Structural highlights

2z2s is a 8 chain structure with sequence from Rhos4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	2q1z
Gene:	rpoE (RHOS4), chrR (RHOS4)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RPOE_RHOS4] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by a cognate anti-sigma factor until released. Sigma-E controls a transcriptional response to singlet oxygen, a by-product of photosynthesis; its continuous activity requires constant exposure to singlet oxygen. The regulon has about 180 genes that protect against or repair damage induced by singlet oxygen, including itself and rpoH2, a heat shock-responsive sigma factor.^[1] ^[2] ^[3] [CHRR_RHOS4] Anti-sigma factor that inhibits the activity of the extracytoplasmic function (ECF) sigma-E factor (RpoE), thereby indirectly regulating the transcription of the cycA and rpoE genes. ECF sigma factors are held in an inactive form by a cognate anti-sigma factor.^[4] ^[5] ^[6]

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

A transcriptional response to singlet oxygen in Rhodobacter sphaeroides is controlled by the group IV sigma factor sigma(E) and its cognate anti-sigma ChrR. Crystal structures of the sigma(E)/ChrR complex reveal a modular, two-domain architecture for ChrR. The ChrR N-terminal anti-sigma domain (ASD) binds a Zn(2+) ion, contacts sigma(E), and is sufficient to inhibit sigma(E)-dependent transcription. The ChrR C-terminal domain adopts a cupin fold, can coordinate an additional Zn(2+), and is required for the transcriptional response to singlet oxygen. Structure-based sequence analyses predict that the ASD defines a common structural fold among predicted group IV anti-sigmas. These ASDs are fused to diverse C-terminal domains that are likely involved in responding to specific environmental signals that control the activity of their cognate sigma factor.

A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria.,Campbell EA, Greenwell R, Anthony JR, Wang S, Lim L, Das K, Sofia HJ, Donohue TJ, Darst SA Mol Cell. 2007 Sep 7;27(5):793-805. PMID:17803943^[7]

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

References

↑ Newman JD, Anthony JR, Donohue TJ. The importance of zinc-binding to the function of Rhodobacter sphaeroides ChrR as an anti-sigma factor. J Mol Biol. 2001 Oct 26;313(3):485-99. PMID:11676534 doi:http://dx.doi.org/10.1006/jmbi.2001.5069
↑ Anthony JR, Warczak KL, Donohue TJ. A transcriptional response to singlet oxygen, a toxic byproduct of photosynthesis. Proc Natl Acad Sci U S A. 2005 May 3;102(18):6502-7. Epub 2005 Apr 26. PMID:15855269 doi:http://dx.doi.org/10.1073/pnas.0502225102
↑ Campbell EA, Greenwell R, Anthony JR, Wang S, Lim L, Das K, Sofia HJ, Donohue TJ, Darst SA. A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria. Mol Cell. 2007 Sep 7;27(5):793-805. PMID:17803943 doi:10.1016/j.molcel.2007.07.009
↑ Newman JD, Anthony JR, Donohue TJ. The importance of zinc-binding to the function of Rhodobacter sphaeroides ChrR as an anti-sigma factor. J Mol Biol. 2001 Oct 26;313(3):485-99. PMID:11676534 doi:http://dx.doi.org/10.1006/jmbi.2001.5069
↑ Anthony JR, Warczak KL, Donohue TJ. A transcriptional response to singlet oxygen, a toxic byproduct of photosynthesis. Proc Natl Acad Sci U S A. 2005 May 3;102(18):6502-7. Epub 2005 Apr 26. PMID:15855269 doi:http://dx.doi.org/10.1073/pnas.0502225102
↑ Campbell EA, Greenwell R, Anthony JR, Wang S, Lim L, Das K, Sofia HJ, Donohue TJ, Darst SA. A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria. Mol Cell. 2007 Sep 7;27(5):793-805. PMID:17803943 doi:10.1016/j.molcel.2007.07.009
↑ Campbell EA, Greenwell R, Anthony JR, Wang S, Lim L, Das K, Sofia HJ, Donohue TJ, Darst SA. A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria. Mol Cell. 2007 Sep 7;27(5):793-805. PMID:17803943 doi:10.1016/j.molcel.2007.07.009

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2z2s"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Rhodobacter sphaeroides SigE in complex with the anti-sigma ChrR==
 <StructureSection load='2z2s' size='340' side='right' caption='[[2z2s]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2z2s]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides_2.4.1 Rhodobacter sphaeroides 2.4.1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z2S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Z2S FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2z2s]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhos4 Rhos4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z2S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Z2S FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2q1z|2q1z]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpoE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272943 Rhodobacter sphaeroides 2.4.1]), chrR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272943 Rhodobacter sphaeroides 2.4.1])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpoE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272943 RHOS4]), chrR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272943 RHOS4])</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=2z2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z2s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2z2s RCSB], [http://www.ebi.ac.uk/pdbsum/2z2s 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=2z2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z2s OCA], [http://pdbe.org/2z2s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2z2s RCSB], [http://www.ebi.ac.uk/pdbsum/2z2s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2z2s ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q3IYV6_RHOS4 Q3IYV6_RHOS4]] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by a cognate anti-sigma factor until released. Sigma-E controls a transcriptional response to singlet oxygen, a by-product of photosynthesis; its continuous activity requires constant exposure to singlet oxygen. The regulon has about 180 genes that protect against or repair damage induced by singlet oxygen, including itself and rpoH2, a heat shock-responsive sigma factor.<ref>PMID:11676534</ref> <ref>PMID:15855269</ref> <ref>PMID:17803943</ref>  [[http://www.uniprot.org/uniprot/CHRR_RHOS4 CHRR_RHOS4]] Anti-sigma factor that inhibits the activity of the extracytoplasmic function (ECF) sigma-E factor (RpoE), thereby indirectly regulating the transcription of the cycA and rpoE genes. ECF sigma factors are held in an inactive form by a cognate anti-sigma factor.<ref>PMID:11676534</ref> <ref>PMID:15855269</ref> <ref>PMID:17803943</ref>
+[[http://www.uniprot.org/uniprot/RPOE_RHOS4 RPOE_RHOS4]] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by a cognate anti-sigma factor until released. Sigma-E controls a transcriptional response to singlet oxygen, a by-product of photosynthesis; its continuous activity requires constant exposure to singlet oxygen. The regulon has about 180 genes that protect against or repair damage induced by singlet oxygen, including itself and rpoH2, a heat shock-responsive sigma factor.<ref>PMID:11676534</ref> <ref>PMID:15855269</ref> <ref>PMID:17803943</ref>  [[http://www.uniprot.org/uniprot/CHRR_RHOS4 CHRR_RHOS4]] Anti-sigma factor that inhibits the activity of the extracytoplasmic function (ECF) sigma-E factor (RpoE), thereby indirectly regulating the transcription of the cycA and rpoE genes. ECF sigma factors are held in an inactive form by a cognate anti-sigma factor.<ref>PMID:11676534</ref> <ref>PMID:15855269</ref> <ref>PMID:17803943</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 20: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2z2s ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 30: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2z2s" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Rhodobacter sphaeroides 2 4.1]]
+[[Category: Rhos4]]
 [[Category: Campbell, E A]]
 [[Category: Darst, S A]]

2z2s

From Proteopedia

Revision as of 04:48, 5 August 2016

Crystal Structure of Rhodobacter sphaeroides SigE in complex with the anti-sigma ChrR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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