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| | <StructureSection load='5fgm' size='340' side='right'caption='[[5fgm]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='5fgm' size='340' side='right'caption='[[5fgm]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fgm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strco Strco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FGM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FGM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fgm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FGM FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sigR, SCO5216 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=100226 STRCO])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5fgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fgm OCA], [http://pdbe.org/5fgm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fgm RCSB], [http://www.ebi.ac.uk/pdbsum/5fgm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fgm 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=5fgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fgm OCA], [https://pdbe.org/5fgm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fgm RCSB], [https://www.ebi.ac.uk/pdbsum/5fgm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fgm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SIGR_STRCO SIGR_STRCO]] 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 an anti-sigma factor (RsrA) until released. Responds to thiol-oxidative stress, involved in regulation of about 30 genes and operons, including the thioredoxin system (trxB-trxA, trxC), ribosomal protein L31, RNA polymerase-binding protein RbpA and mycothiol (MSH) biosynthetic (mshA) and recycling genes (mca). In conjunction with its cognate anti-sigma factor RsrA may sense the intracellular level of reduced MSH.<ref>PMID:10428967</ref> <ref>PMID:11737643</ref> <ref>PMID:14529630</ref> <ref>PMID:9755177</ref> | + | [https://www.uniprot.org/uniprot/SIGR_STRCO SIGR_STRCO] 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 an anti-sigma factor (RsrA) until released. Responds to thiol-oxidative stress, involved in regulation of about 30 genes and operons, including the thioredoxin system (trxB-trxA, trxC), ribosomal protein L31, RNA polymerase-binding protein RbpA and mycothiol (MSH) biosynthetic (mshA) and recycling genes (mca). In conjunction with its cognate anti-sigma factor RsrA may sense the intracellular level of reduced MSH.<ref>PMID:10428967</ref> <ref>PMID:11737643</ref> <ref>PMID:14529630</ref> <ref>PMID:9755177</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Strco]]
| + | [[Category: Park SY]] |
| - | [[Category: Park, S Y]] | + | |
| - | [[Category: Ecf sigma factor]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Promoter -35 element binding]]
| + | |
| - | [[Category: Sigma factor region 4]]
| + | |
| Structural highlights
Function
SIGR_STRCO 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 an anti-sigma factor (RsrA) until released. Responds to thiol-oxidative stress, involved in regulation of about 30 genes and operons, including the thioredoxin system (trxB-trxA, trxC), ribosomal protein L31, RNA polymerase-binding protein RbpA and mycothiol (MSH) biosynthetic (mshA) and recycling genes (mca). In conjunction with its cognate anti-sigma factor RsrA may sense the intracellular level of reduced MSH.[1] [2] [3] [4]
Publication Abstract from PubMed
In Gram-positive Streptomyces coelicolor A3(2), SigR (Sc sigma(R)) of the group IV ECF sigma factor singly activates expression of more than 30 oxidation responsive genes. Of the two promoter-binding domains - individually called region 2 and region 4 - within Sc sigma(R), we hereby report a 2.6 A resolution structure of the -35 element interacting carboxyl-terminal region 4 (Sc sigma(R)4). Structural comparison of Sc sigma(R)4 with the Escherichia coli SigE (Ec sigma(E)) in complex with Ec sigma(E) -35 element suggested that a single residue (Sc sigma(R) Met188 and Ec sigma(E) Arg171) may be responsible for distinguishing the one-base pair difference of the -35 elements - Sc sigma(R)(-31')ATTCC(-35') ((-31')A) vs. Ec sigma(E)(-31')GTTCC(-35') ((-31')G) - by interacting with the -31'-base. Further studies using expressed Sc sigma(R) indicate that the wild-type Sc sigma(R) with Met188 selectively interacted with the (-31')A sequence over the (-31')G sequence, whereas a mutation of Met188 to arginine resulted in interaction with both (-31')A and (-31')G sequences. Hence, we conclude that Met188 of Sc sigma(R) confers the (-31')A-selectivity in -35 element interaction by disfavoured interaction with the (-31')G base.
In Streptomyces coelicolor SigR, methionine at the -35 element interacting region 4 confers the -31'-adenine base selectivity.,Kim KY, Park JK, Park S Biochem Biophys Res Commun. 2016 Feb 5;470(2):257-62. doi:, 10.1016/j.bbrc.2016.01.075. Epub 2016 Jan 14. PMID:26775842[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kang JG, Paget MS, Seok YJ, Hahn MY, Bae JB, Hahn JS, Kleanthous C, Buttner MJ, Roe JH. RsrA, an anti-sigma factor regulated by redox change. EMBO J. 1999 Aug 2;18(15):4292-8. PMID:10428967 doi:http://dx.doi.org/10.1093/emboj/18.15.4292
- ↑ Paget MS, Molle V, Cohen G, Aharonowitz Y, Buttner MJ. Defining the disulphide stress response in Streptomyces coelicolor A3(2): identification of the sigmaR regulon. Mol Microbiol. 2001 Nov;42(4):1007-20. PMID:11737643
- ↑ Li W, Bottrill AR, Bibb MJ, Buttner MJ, Paget MS, Kleanthous C. The Role of zinc in the disulphide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor. J Mol Biol. 2003 Oct 17;333(2):461-72. PMID:14529630 doi:http://dx.doi.org/10.1016/S0022283603010763
- ↑ Paget MS, Kang JG, Roe JH, Buttner MJ. sigmaR, an RNA polymerase sigma factor that modulates expression of the thioredoxin system in response to oxidative stress in Streptomyces coelicolor A3(2). EMBO J. 1998 Oct 1;17(19):5776-82. PMID:9755177 doi:http://dx.doi.org/10.1093/emboj/17.19.5776
- ↑ Kim KY, Park JK, Park S. In Streptomyces coelicolor SigR, methionine at the -35 element interacting region 4 confers the -31'-adenine base selectivity. Biochem Biophys Res Commun. 2016 Feb 5;470(2):257-62. doi:, 10.1016/j.bbrc.2016.01.075. Epub 2016 Jan 14. PMID:26775842 doi:http://dx.doi.org/10.1016/j.bbrc.2016.01.075
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