Literature DB >> 19636956

NMR assignment and secondary structure of the STAS domain of Rv1739c, a putative sulfate transporter of Mycobacterium tuberculosis.

Alok K Sharma1, Liwen Ye, Alexander S Zolotarev, Seth L Alper, Alan C Rigby.   

Abstract

We report (1)H(N), (15)N, and (13)C resonance assignments for the 15.6 kDa STAS domain of the putative sulfate transporter of Mycobacterium tuberculosis, Rv1739c, using heteronuclear, multidimensional NMR spectroscopy. Rv1739c is a SulP anion permease, related in structure to the SLC26 gene family of metazoan anion exchangers and anion channels.

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Year:  2009        PMID： 19636956     DOI： 10.1007/s12104-009-9150-z

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN： 1874-270X            Impact factor:   0.746


  3 in total

1.  Guanine nucleotides differentially modulate backbone dynamics of the STAS domain of the SulP/SLC26 transport protein Rv1739c of Mycobacterium tuberculosis.

Authors:  Alok K Sharma; Liwen Ye; Seth L Alper; Alan C Rigby
Journal:  FEBS J       Date:  2011-12-22       Impact factor: 5.542

2.  Solution structure of the guanine nucleotide-binding STAS domain of SLC26-related SulP protein Rv1739c from Mycobacterium tuberculosis.

Authors:  Alok K Sharma; Liwen Ye; Christina E Baer; Kumaran Shanmugasundaram; Tom Alber; Seth L Alper; Alan C Rigby
Journal:  J Biol Chem       Date:  2010-12-29       Impact factor: 5.157

3.  Human SLC26A4/Pendrin STAS domain is a nucleotide-binding protein: Refolding and characterization for structural studies.

Authors:  Alok K Sharma; Tobias Krieger; Alan C Rigby; Israel Zelikovic; Seth L Alper
Journal:  Biochem Biophys Rep       Date:  2016-08-26
  3 in total

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