Structural highlights
Function
P71817_MYCTO
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 A 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 alpha + beta 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 17beta-estradiol 17-hemisuccinate (EH) have also been solved and analyzed.
Crystal structure of Mycobacterium tuberculosis Rv0760c at 1.50 A resolution, a structural homolog of Delta(5)-3-ketosteroid isomerase.,Cherney MM, Garen CR, James MN Biochim Biophys Acta. 2008 Nov;1784(11):1625-32. Epub 2008 Jun 6. PMID:18589008[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cherney MM, Garen CR, James MN. Crystal structure of Mycobacterium tuberculosis Rv0760c at 1.50 A resolution, a structural homolog of Delta(5)-3-ketosteroid isomerase. Biochim Biophys Acta. 2008 Nov;1784(11):1625-32. Epub 2008 Jun 6. PMID:18589008 doi:10.1016/j.bbapap.2008.05.012