Crystallization and preliminary X-ray diffraction studies of an alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis.
alpha-Methylacyl-CoA racemase is a key enzyme in the metabolism of 2-methyl-branched fatty acids and, in mammals, in the conversion of cholesterol to bile acids. The enzyme from Mycobacterium tuberculosis has been purified to homogeneity and crystallized by the hanging-drop vapour-diffusion method. The crystals of the unliganded racemase belong to space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 122.0, c = 256.4 A. Data sets were collected at 100 K. The crystals diffract to 2.8 A using synchrotron radiation.
Bhaumik
Prasenjit
P
Biocenter Oulu and Department of Biochemistry, University of Oulu, Linnanmaa, Box 3000, FIN-90014 Oulu, Finland.
Kursula
Petri
P
Ratas
Ville
V
Conzelmann
Ernst
E
Hiltunen
J Kalervo
JK
Schmitz
Werner
W
Wierenga
Rik K
RK
D000595:Amino Acid Sequence; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D019998:Racemases and Epimerases / Q000737:chemistry* / Q000378:metabolism; D051381:Rats; D017386:Sequence Homology, Amino Acid; D017356:Synchrotrons
D019998:Racemases and Epimerases; C108352:alpha-methylacyl-CoA racemase