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2Z77

X-ray crystal structure of RV0760c from Mycobacterium tuberculosis in complex with estradiol-17beta-hemisuccinate

Summary for 2Z77
Entry DOI10.2210/pdb2z77/pdb
Related2A15 2Z76 2Z7A
DescriptorPutative steroid isomerase, 4-{[(14beta,17alpha)-3-hydroxyestra-1,3,5(10)-trien-17-yl]oxy}-4-oxobutanoic acid, ACETATE ION, ... (5 entities in total)
Functional Keywordsalpha+beta conical barrel, complex with estradiol-17beta-hemisuccinate, structural genomics, tb structural genomics consortium, tbsgc, isomerase
Biological sourceMycobacterium tuberculosis
Total number of polymer chains4
Total formula weight62381.60
Authors
Cherney, M.M.,Garen, C.R.,James, M.N.G.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2007-08-16, release date: 2007-09-18, Last modification date: 2023-08-30)
Primary citationCherney, M.M.,Garen, C.R.,James, M.N.
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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.03 Å)
Structure validation

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