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| | ==Solution Structure of putative anti sigma factor antagonist from Thermotoga maritima (TM1442)== | | ==Solution Structure of putative anti sigma factor antagonist from Thermotoga maritima (TM1442)== |
| - | <StructureSection load='1sbo' size='340' side='right'caption='[[1sbo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1sbo' size='340' side='right'caption='[[1sbo]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1sbo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SBO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SBO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1sbo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SBO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SBO FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1auz|1auz]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM1442 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</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=1sbo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sbo OCA], [https://pdbe.org/1sbo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sbo RCSB], [https://www.ebi.ac.uk/pdbsum/1sbo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sbo ProSAT], [https://www.topsan.org/Proteins/JCSG/1sbo TOPSAN]</span></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=1sbo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sbo OCA], [http://pdbe.org/1sbo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sbo RCSB], [http://www.ebi.ac.uk/pdbsum/1sbo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sbo ProSAT], [http://www.topsan.org/Proteins/JCSG/1sbo TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Y1442_THEMA Y1442_THEMA]] In the phosphorylated form it could act as an anti-anti-sigma factor that counteracts an anti-sigma factor and thus releases a sigma factor from inhibition (By similarity). | + | [https://www.uniprot.org/uniprot/Y1442_THEMA Y1442_THEMA] In the phosphorylated form it could act as an anti-anti-sigma factor that counteracts an anti-sigma factor and thus releases a sigma factor from inhibition (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43589]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Etezady-Esfarjaini, T]] | + | [[Category: Thermotoga maritima]] |
| - | [[Category: Herrmann, T]] | + | [[Category: Etezady-Esfarjaini T]] |
| - | [[Category: Structural genomic]] | + | [[Category: Herrmann T]] |
| - | [[Category: Lesley, S A]] | + | [[Category: Lesley SA]] |
| - | [[Category: Placzek, W J]] | + | [[Category: Placzek WJ]] |
| - | [[Category: Wuthrich, K]] | + | [[Category: Wuthrich K]] |
| - | [[Category: Jcsg]]
| + | |
| - | [[Category: Open sandwich]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
Y1442_THEMA In the phosphorylated form it could act as an anti-anti-sigma factor that counteracts an anti-sigma factor and thus releases a sigma factor from inhibition (By similarity).
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
The NMR structures of the unphosphorylated Thermotoga maritima protein TM1442 at pH 4.8 and of the phosphorylated TM1442 (TM1442-P) at pH 7.0 are presented, and a functional interaction of TM1442 with TM0733 is characterized. Although the NMR spectra of TM1442-P at pH 7.0 are of high quality, detailed NMR studies of unphosphorylated TM1442 could be performed only at slightly acidic pH values and high salt concentration. TM1442 is a putative anti-sigma-factor antagonist related to the sigmaF and sigmaB regulation systems in Bacillus subtilis, which is the component in this system that can be phosphorylated. The kinase TM0733, which shows sequence similarity to the GHKL ATPase/kinase superfamily, was identified as the possible anti-sigma-factor of TM1442 using a bioinformatics analysis. Phosphorylation of TM1442 by TM0733 was confirmed by NMR, mass spectroscopy and native gel electrophoresis, and Ser59 was identified as the phosphorylation site using site-directed mutational analysis. The solution structure of TM1442-P at pH 7.0 has the same global fold as free TM1442 at pH 4.8, with an alpha/beta topology consisting of a central four-stranded beta sheet and three alpha helices, but the regular secondary structure elements wrapping the hydrophobic core of the protein undergo subtle conformational changes upon phosphorylation.
Solution structures of the putative anti-sigma-factor antagonist TM1442 from Thermotoga maritima in the free and phosphorylated states.,Etezady-Esfarjani T, Placzek WJ, Herrmann T, Wuthrich K Magn Reson Chem. 2006 Jul;44 Spec No:S61-70. PMID:16826544[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Etezady-Esfarjani T, Placzek WJ, Herrmann T, Wuthrich K. Solution structures of the putative anti-sigma-factor antagonist TM1442 from Thermotoga maritima in the free and phosphorylated states. Magn Reson Chem. 2006 Jul;44 Spec No:S61-70. PMID:16826544 doi:10.1002/mrc.1831
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