2kln

</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>

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== 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>

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== References ==

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