NMR assignment and secondary structure of the STAS domain of Rv1739c, a putative sulfate transporter of Mycobacterium tuberculosis.
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.
Sharma
Alok K
AK
Division of Molecular Vascular Medicine, Center for Vascular Biology Research, Beth Israel Deaconess Medical Center, RN-231 99 Brookline Ave, Boston, MA 02215, USA.
Ye
Liwen
L
Zolotarev
Alexander S
AS
Alper
Seth L
SL
Rigby
Alan C
AC
D000595:Amino Acid Sequence; D027321:Anion Transport Proteins / Q000737:chemistry*; D002247:Carbon Isotopes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000737:chemistry*; D009587:Nitrogen Isotopes / Q000737:chemistry; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D011522:Protons
D027321:Anion Transport Proteins; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D021122:Protein Subunits; D011522:Protons