2A15

X-ray Crystal Structure of RV0760 from Mycobacterium Tuberculosis at 1.68 Angstrom Resolution

Summary for 2A15

• Entry DOI: 10.2210/pdb2a15/pdb
• Descriptor: HYPOTHETICAL PROTEIN Rv0760c, NICOTINAMIDE (3 entities in total)
• Functional Keywords: beta-alpha-barrel, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, unknown function
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 15378.13

Authors

Garen, C.R.,Cherney, M.M.,James, M.N.G.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2005-06-17, release date: 2005-10-11, Last modification date: 2024-04-03)

Primary citation

Cherney, M.M.,Garen, C.R.,James, M.N.G.
Crystal structure of Mycobacterium tuberculosis Rv0760c at 1.50 A resolution, a structural homolog of Delta(5)-3-ketosteroid isomerase
Biochim.Biophys.Acta, 1784:1625-1632, 2008

PubMed 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 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.

PubMed: 18589008
DOI: 10.1016/j.bbapap.2008.05.012

Experimental method

X-RAY DIFFRACTION (1.68 Å)