2DZD

Crystal structure of the biotin carboxylase domain of pyruvate carboxylase

2DZD の概要

• エントリーDOI: 10.2210/pdb2dzd/pdb
• 分子名称: pyruvate carboxylase (2 entities in total)
• 機能のキーワード: biotin carboxylase, pyruvate carboxylase, bacillus thermodenitrificans, ligase
• 由来する生物種: Geobacillus thermodenitrificans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 102806.81

構造登録者

Kondo, S.,Nakajima, Y.,Sugio, S.,Sueda, S.,Islam, M.N.,Kondo, H. (登録日: 2006-09-27, 公開日: 2007-09-25, 最終更新日: 2023-10-25)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)