Abstract
We have determined the X-ray crystal structure of the Mycobacterium tuberculosis ( Mtb) gene product encoded by the open reading frame Rv0760c at 1.50 Å resolution by single-wavelength anomalous dispersion (SAD) phasing of diffraction data from crystals of the selenomethionine-substituted protein. Refinement against diffraction data from the native protein resulted in R work = 19.5% and R free = 21.4%. The X-ray crystal structure shows that the homodimeric Rv0760c polypeptide has an α + β conical barrel fold placing it among many structural neighbors of the nuclear transport factor 2 family (NTF2). This family is highly conserved in terms of structure; however the substrates and individual protein functions are diverse. The structures of native Rv0760c in several different crystal forms and Rv0760c bound to 17β-estradiol 17-hemisuccinate (EH) have also been solved and analyzed.
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