Crystallization and preliminary X-ray analysis of the 12S central subunit of transcarboxylase from Propionibacterium shermanii.
The hexameric 12S central subunit of transcarboxylase has been crystallized in both free and substrate-bound forms. The apo crystals belong to the cubic space group P4(2)32, with unit-cell parameters a = b = c = 188.5 A, and diffract to 3.5 A resolution. Crystals of two substrate-bound complexes, 12S with methylmalonyl CoA and 12S with malonyl CoA, are isomorphous and belong to space group C2, with unit-cell parameters a = 115.5, b = 201.4, c = 146.9 A, beta = 102.7 degrees. These crystals diffract to 1.9 A resolution with synchrotron radiation. Two useful heavy-atom phasing derivatives of methylmalonyl CoA-bound crystals have been obtained by co-crystallization or crystal soaking.
Wang
Y F
YF
Department of Molecular Cardiology and Center for Structural Biology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH 44195, USA.
Hyatt
D C
DC
Rivera
R E
RE
Carey
P R
PR
Yee
V C
VC
D000214:Acyl Coenzyme A / Q000378:metabolism; D019878:Carboxyl and Carbamoyl Transferases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D008316:Malonyl Coenzyme A / Q000378:metabolism; D008970:Molecular Weight; D011424:Propionibacterium / Q000201:enzymology*; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D017384:Sequence Deletion; D017356:Synchrotrons
D000214:Acyl Coenzyme A; D021122:Protein Subunits; D011994:Recombinant Proteins; C015357:methylmalonyl-coenzyme A; D008316:Malonyl Coenzyme A; D019878:Carboxyl and Carbamoyl Transferases; C021580:Methylmalonyl-CoA carboxytransferase