2KLN

Solution Structure of STAS domain of RV1739c from M. tuberculosis

2KLN の概要

• エントリーDOI: 10.2210/pdb2kln/pdb
• 分子名称: PROBABLE SULPHATE-TRANSPORT TRANSMEMBRANE PROTEIN, COG0659 (1 entity in total)
• 機能のキーワード: slc26, sulfate, sulp, antisigma factor antagonist, ensemble of 25 structures, membrane, transmembrane, transport protein
• 由来する生物種: Mycobacterium bovis
• 細胞内の位置: Membrane; Multi-pass membrane protein (By similarity): Q7TZN7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15093.15

構造登録者

Sharma, A.K.,Ye, L.,Zolotarev, A.S.,Alper, S.L.,Rigby, A.C. (登録日: 2009-07-06, 公開日: 2010-12-15, 最終更新日: 2024-05-01)

主引用文献

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

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: 21190940
DOI: 10.1074/jbc.M110.165449

実験手法

SOLUTION NMR