1or7: Difference between revisions

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<StructureSection load='1or7' size='340' side='right'caption='[[1or7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1or7' size='340' side='right'caption='[[1or7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1or7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OR7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OR7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1or7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OR7 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPOE OR SIGE OR B2573 OR C3097 OR Z3855 OR ECS3439 OR SF2635 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), RSEA OR MCLA OR B2572 OR C3096 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1or7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or7 OCA], [http://pdbe.org/1or7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1or7 RCSB], [http://www.ebi.ac.uk/pdbsum/1or7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1or7 ProSAT]</span></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=1or7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or7 OCA], [https://pdbe.org/1or7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1or7 RCSB], [https://www.ebi.ac.uk/pdbsum/1or7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1or7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/RPOE_ECOLI RPOE_ECOLI]] Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment. The 90 member regulon consists of the genes necessary for the synthesis and maintenance of both proteins and LPS of the outer membrane.<ref>PMID:7889935</ref> <ref>PMID:7889934</ref> <ref>PMID:2691330</ref> <ref>PMID:9159522</ref> <ref>PMID:9159523</ref> <ref>PMID:16336047</ref> [[http://www.uniprot.org/uniprot/RSEA_ECOLI RSEA_ECOLI]] Negative regulator of RpoE.
[https://www.uniprot.org/uniprot/RPOE_ECOLI RPOE_ECOLI] Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment. The 90 member regulon consists of the genes necessary for the synthesis and maintenance of both proteins and LPS of the outer membrane.<ref>PMID:7889935</ref> <ref>PMID:7889934</ref> <ref>PMID:2691330</ref> <ref>PMID:9159522</ref> <ref>PMID:9159523</ref> <ref>PMID:16336047</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1or7 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=1or7 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The sigma factors are the key regulators of bacterial transcription. ECF (extracytoplasmic function) sigma's are the largest and most divergent group of sigma(70) family members. ECF sigma's are normally sequestered in an inactive complex by their specific anti-sigma factor, which often spans the inner membrane. Here, we determined the 2 A resolution crystal structure of the Escherichia coli ECF sigma factor sigma(E) in an inhibitory complex with the cytoplasmic domain of its anti-sigma, RseA. Despite extensive sequence variability, the two major domains of sigma(E) are virtually identical in structure to the corresponding domains of other sigma(70) family members. In combination with a model of the sigma(E) holoenzyme and biochemical data, the structure reveals that RseA functions by sterically occluding the two primary binding determinants on sigma(E) for core RNA polymerase.
Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain of its anti-sigma RseA.,Campbell EA, Tupy JL, Gruber TM, Wang S, Sharp MM, Gross CA, Darst SA Mol Cell. 2003 Apr;11(4):1067-78. PMID:12718891<ref>PMID:12718891</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1or7" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Campbell, E A]]
[[Category: Campbell EA]]
[[Category: Darst, S A]]
[[Category: Darst SA]]
[[Category: Gross, C A]]
[[Category: Gross CA]]
[[Category: Gruber, T M]]
[[Category: Gruber TM]]
[[Category: Sharp, M M]]
[[Category: Sharp MM]]
[[Category: Tupy, J L]]
[[Category: Tupy JL]]
[[Category: Wang, S]]
[[Category: Wang S]]
[[Category: Dna-binding]]
[[Category: Regulation]]
[[Category: Transcription]]
[[Category: Transmembrane]]

Latest revision as of 11:02, 14 February 2024

Crystal Structure of Escherichia coli sigmaE with the Cytoplasmic Domain of its Anti-sigma RseACrystal Structure of Escherichia coli sigmaE with the Cytoplasmic Domain of its Anti-sigma RseA

Structural highlights

1or7 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RPOE_ECOLI Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment. The 90 member regulon consists of the genes necessary for the synthesis and maintenance of both proteins and LPS of the outer membrane.[1] [2] [3] [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.

See Also

References

  1. ↑ Raina S, Missiakas D, Georgopoulos C. The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli. EMBO J. 1995 Mar 1;14(5):1043-55. PMID:7889935
  2. ↑ Rouviere PE, De Las Penas A, Mecsas J, Lu CZ, Rudd KE, Gross CA. rpoE, the gene encoding the second heat-shock sigma factor, sigma E, in Escherichia coli. EMBO J. 1995 Mar 1;14(5):1032-42. PMID:7889934
  3. ↑ Erickson JW, Gross CA. Identification of the sigma E subunit of Escherichia coli RNA polymerase: a second alternate sigma factor involved in high-temperature gene expression. Genes Dev. 1989 Sep;3(9):1462-71. PMID:2691330
  4. ↑ Missiakas D, Mayer MP, Lemaire M, Georgopoulos C, Raina S. Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins. Mol Microbiol. 1997 Apr;24(2):355-71. PMID:9159522
  5. ↑ De Las Penas A, Connolly L, Gross CA. The sigmaE-mediated response to extracytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of sigmaE. Mol Microbiol. 1997 Apr;24(2):373-85. PMID:9159523
  6. ↑ Rhodius VA, Suh WC, Nonaka G, West J, Gross CA. Conserved and variable functions of the sigmaE stress response in related genomes. PLoS Biol. 2006 Jan;4(1):e2. PMID:16336047 doi:http://dx.doi.org/10.1371/journal.pbio.0040002

1or7, resolution 2.00Å

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