2KLN
Solution Structure of STAS domain of RV1739c from M. tuberculosis
Summary for 2KLN
| Entry DOI | 10.2210/pdb2kln/pdb |
| Descriptor | PROBABLE SULPHATE-TRANSPORT TRANSMEMBRANE PROTEIN, COG0659 (1 entity in total) |
| Functional Keywords | slc26, sulfate, sulp, antisigma factor antagonist, ensemble of 25 structures, membrane, transmembrane, transport protein |
| Biological source | Mycobacterium bovis |
| Cellular location | Membrane; Multi-pass membrane protein (By similarity): Q7TZN7 |
| Total number of polymer chains | 1 |
| Total formula weight | 15093.15 |
| Authors | Sharma, A.K.,Ye, L.,Zolotarev, A.S.,Alper, S.L.,Rigby, A.C. (deposition date: 2009-07-06, release date: 2010-12-15, Last modification date: 2024-05-01) |
| Primary citation | Sharma, A.K.,Ye, L.,Baer, C.E.,Shanmugasundaram, K.,Alber, T.,Alper, S.L.,Rigby, A.C. Solution Structure of the Guanine Nucleotide-binding STAS Domain of SLC26-related SulP Protein Rv1739c from Mycobacterium tuberculosis. J.Biol.Chem., 286:8534-8544, 2011 Cited by PubMed Abstract: 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-Å root mean square deviation structure revealed a four-stranded β-sheet with five interspersed α-helices, resembling the anti-σ 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-σ factors. These results demonstrate that Rv1739c STAS binds guanine nucleotides at physiological concentrations and undergoes a ligand-induced conformational change but, unlike anti-σ factor antagonists, may not mediate signals via phosphorylation. PubMed: 21190940DOI: 10.1074/jbc.M110.165449 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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