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| - | [[Image:2h27.gif|left|200px]]<br /><applet load="2h27" size="350" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="2h27, resolution 2.30Å" /> | |
| - | '''Crystal Structure of Escherichia coli SigmaE Region 4 Bound to its-35 Element DNA'''<br /> | |
| | | | |
| - | ==Overview== | + | ==Crystal Structure of Escherichia coli SigmaE Region 4 Bound to its-35 Element DNA== |
| - | The control of bacterial transcription initiation depends on a primary, sigma factor for housekeeping functions, as well as alternative sigma, factors that control regulons in response to environmental stresses. The, largest and most diverse subgroup of alternative sigma factors, the group, IV extracytoplasmic function sigma factors, directs the transcription of, genes that regulate a wide variety of responses, including envelope stress, and pathogenesis. We determined the 2.3-A resolution crystal structure of, the -35 element recognition domain of a group IV sigma factor, Escherichia, coli sigma(E)4, bound to its consensus -35 element, GGAACTT. Despite, similar function and secondary structure, the primary and group IV sigma, factors recognize their -35 elements using distinct mechanisms. Conserved, sequence elements of the sigma(E) -35 element induce a DNA geometry, characteristic of AA/TT-tract DNA, including a rigid, straight, double-helical axis and a narrow minor groove. For this reason, the highly, conserved AA in the middle of the GGAACTT motif is essential for -35, element recognition by sigma(E)4, despite the absence of direct, protein-DNA interactions with these DNA bases. These principles of, sigma(E)4/-35 element recognition can be applied to a wide range of other, group IV sigma factors.
| + | <StructureSection load='2h27' size='340' side='right'caption='[[2h27]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | + | == Structural highlights == |
| | + | <table><tr><td colspan='2'>[[2h27]] is a 6 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=2H27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H27 FirstGlance]. <br> |
| | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></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=2h27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h27 OCA], [https://pdbe.org/2h27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h27 RCSB], [https://www.ebi.ac.uk/pdbsum/2h27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h27 ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [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 == |
| | + | [[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/h2/2h27_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=2h27 ConSurf]. |
| | + | <div style="clear:both"></div> |
| | | | |
| - | ==About this Structure== | + | ==See Also== |
| - | 2H27 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H27 OCA].
| + | *[[Sigma factor 3D structures|Sigma factor 3D structures]] |
| - | | + | == References == |
| - | ==Reference== | + | <references/> |
| - | The structural basis for promoter -35 element recognition by the group IV sigma factors., Lane WJ, Darst SA, PLoS Biol. 2006 Sep;4(9):e269. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16903784 16903784]
| + | __TOC__ |
| - | [[Category: Escherichia coli]] | + | </StructureSection> |
| - | [[Category: Single protein]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Darst, S.A.]] | + | [[Category: Large Structures]] |
| - | [[Category: Lane, W.J.]] | + | [[Category: Darst SA]] |
| - | [[Category: MPD]]
| + | [[Category: Lane WJ]] |
| - | [[Category: double helix]]
| + | |
| - | [[Category: helix-turn-helix]]
| + | |
| - | [[Category: protein-dna complex]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:24:00 2008''
| + | |
| Structural highlights
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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
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