2kln
From Proteopedia
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==Solution Structure of STAS domain of RV1739c from M. tuberculosis== | ==Solution Structure of STAS domain of RV1739c from M. tuberculosis== | ||
- | <StructureSection load='2kln' size='340' side='right' caption='[[2kln | + | <StructureSection load='2kln' size='340' side='right'caption='[[2kln]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2kln]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2kln]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_variant_bovis Mycobacterium tuberculosis variant bovis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KLN FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kln OCA], [https://pdbe.org/2kln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kln RCSB], [https://www.ebi.ac.uk/pdbsum/2kln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kln ProSAT]</span></td></tr> |
</table> | </table> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The structure and intrinsic activities of conserved STAS domains of the ubiquitous SulP/SLC26 anion transporter superfamily have until recently remained unknown. Here we report the heteronuclear, multidimensional NMR spectroscopy solution structure of the STAS domain from the SulP/SLC26 putative anion transporter Rv1739c of Mycobacterium tuberculosis. The 0.87-A root mean square deviation structure revealed a four-stranded beta-sheet with five interspersed alpha-helices, resembling the anti-sigma factor antagonist fold. Rv1739c STAS was shown to be a guanine nucleotide-binding protein, as revealed by nucleotide-dependent quench of intrinsic STAS fluorescence and photoaffinity labeling. NMR chemical shift perturbation analysis partnered with in silico docking calculations identified solvent-exposed STAS residues involved in nucleotide binding. Rv1739c STAS was not an in vitro substrate of mycobacterial kinases or anti-sigma factors. These results demonstrate that Rv1739c STAS binds guanine nucleotides at physiological concentrations and undergoes a ligand-induced conformational change but, unlike anti-sigma factor antagonists, may not mediate signals via phosphorylation. | ||
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- | Solution Structure of the Guanine Nucleotide-binding STAS Domain of SLC26-related SulP Protein Rv1739c from Mycobacterium tuberculosis.,Sharma AK, Ye L, Baer CE, Shanmugasundaram K, Alber T, Alper SL, Rigby AC J Biol Chem. 2011 Mar 11;286(10):8534-44. Epub 2010 Dec 29. PMID:21190940<ref>PMID:21190940</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 2kln" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Mycobacterium tuberculosis | + | [[Category: Large Structures]] |
- | [[Category: Alper | + | [[Category: Mycobacterium tuberculosis variant bovis]] |
- | [[Category: Rigby | + | [[Category: Alper SL]] |
- | [[Category: Sharma | + | [[Category: Rigby AC]] |
- | [[Category: Ye | + | [[Category: Sharma AK]] |
- | [[Category: Zolotarev | + | [[Category: Ye L]] |
- | + | [[Category: Zolotarev AS]] | |
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Current revision
Solution Structure of STAS domain of RV1739c from M. tuberculosis
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