ArticleThe Journal of biological chemistry2011
Solution structure of the guanine nucleotide-binding STAS domain of SLC26-related SulP protein Rv1739c from Mycobacterium tuberculosis.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 43 citations in OpenAlex.
- Article
- Structural basis for functional interactions in dimers of SLC26 transporters.Nature communications · 2019Article
- Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery.Molecules (Basel, Switzerland) · 2017Review
- Human SLC26A4/Pendrin STAS domain is a nucleotide-binding protein: Refolding and characterization for structural studies.Biochemistry and biophysics reports · 2016Article
- Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family.Nature structural & molecular biology · 2015Article
- Functional regulation of the SLC26-family protein prestin by calcium/calmodulin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Deciphering the growth behaviour of Mycobacterium africanum.PLoS neglected tropical diseases · 2013Article
- CFTR-SLC26 transporter interactions in epithelia.Biophysical reviews · 2012Article
- Guanine nucleotides differentially modulate backbone dynamics of the STAS domain of the SulP/SLC26 transport protein Rv1739c of Mycobacterium tuberculosis.The FEBS journal · 2012Article
- A phosphorylated pseudokinase complex controls cell wall synthesis in mycobacteria.Science signaling · 2012Article
- Blue news update: BODIPY-GTP binds to the blue-light receptor YtvA while GTP does not.PloS one · 2012Article
- SLC26 anion exchangers of guinea pig pancreatic duct: molecular cloning and functional characterization.American journal of physiology. Cell physiology · 2011Article
- Low resolution structure of a bacterial SLC26 transporter reveals dimeric stoichiometry and mobile intracellular domains.The Journal of biological chemistry · 2011Article
- Analysis of cellular localization and function of carboxy-terminal mutants of pendrin.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2011Article
- STAS domain structure and function.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2011Review
- The SLC26 gene family of anion transporters and channels.Molecular aspects of medicineReview
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Authors and funding
7 authors at 4 institutions in 2 countries.
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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.
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