Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans.
The biotin carboxylase (BC) domain of pyruvate carboxylase (PC) from Bacillus thermodenitrificans (BC-bPC) was crystallized in an orthorhombic form (space group P2(1)2(1)2(1)), with unit-cell parameters a = 79.6, b = 116.0, c = 115.7 A. Two BC protomers are contained in the asymmetric unit. Diffraction data were collected at 100 K and the crystal structure was solved by the molecular-replacement method and refined against reflections in the 20.0-2.4 A resolution range, giving an R factor of 0.235 and a free R factor of 0.292. The overall structure of BC-bPC is similar to those of the BC subunits of Aquifex aeolicus PC (BC-aPC) and Escherichia coli ACC (BC-eACC). The crystal structure revealed that BC-bPC forms a unique dimeric quaternary structure, which might be caused as a result of the division of the BC domain from the rest of the protein. The position of domain B in BC-bPC differs from those in other enzymes of similar structure (BC-aPC and BC-eACC).
Kondo
Shin
S
ZOEGENE Corporation, Aoba, Yokohama 227-8502, Japan. kondo@bio.kyutech.ac.jp
Nakajima
Yoshitaka
Y
Sugio
Shigetoshi
S
Sueda
Shinji
S
Islam
Md Nurul
MN
Kondo
Hiroki
H
D001407:Bacillus / Q000201:enzymology* / Q000235:genetics; D001665:Binding Sites; D019731:Carbon-Nitrogen Ligases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D018360:Crystallography, X-Ray; D019281:Dimerization; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011766:Pyruvate Carboxylase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D055672:Static Electricity
D021122:Protein Subunits; D019731:Carbon-Nitrogen Ligases; C019791:biotin carboxylase; D011766:Pyruvate Carboxylase