2kln: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<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>
<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='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>
</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'>[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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2kln" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
</StructureSection>
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