2DZD

Crystal structure of the biotin carboxylase domain of pyruvate carboxylase

Summary for 2DZD

• Entry DOI: 10.2210/pdb2dzd/pdb
• Descriptor: pyruvate carboxylase (2 entities in total)
• Functional Keywords: biotin carboxylase, pyruvate carboxylase, bacillus thermodenitrificans, ligase
• Biological source: Geobacillus thermodenitrificans
• Total number of polymer chains: 2
• Total formula weight: 102806.81

Authors

Kondo, S.,Nakajima, Y.,Sugio, S.,Sueda, S.,Islam, M.N.,Kondo, H. (deposition date: 2006-09-27, release date: 2007-09-25, Last modification date: 2023-10-25)

Primary citation

Kondo, S.,Nakajima, Y.,Sugio, S.,Sueda, S.,Islam, M.N.,Kondo, H.
Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans
ACTA CRYSTALLOGR.,SECT.D, 63:885-890, 2007

PubMed Abstract: 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).

PubMed: 17642515
DOI: 10.1107/S0907444907029423

Experimental method

X-RAY DIFFRACTION (2.4 Å)