3BG5

Crystal Structure of Staphylococcus Aureus Pyruvate Carboxylase

3BG5 の概要

• エントリーDOI: 10.2210/pdb3bg5/pdb
• 関連するPDBエントリー: 1RQH 3BG3 3BG9
• 分子名称: Pyruvate carboxylase, MANGANESE (II) ION, 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL, ... (5 entities in total)
• 機能のキーワード: tim barrel, atp-binding, ligase, nucleotide-binding, pyruvate
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 527172.23

構造登録者

Xiang, S.,Tong, L. (登録日: 2007-11-26, 公開日: 2008-02-26, 最終更新日: 2023-11-15)

主引用文献

Xiang, S.,Tong, L.
Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction.
Nat.Struct.Mol.Biol., 15:295-302, 2008

PubMed Abstract: Pyruvate carboxylase (PC) catalyzes the biotin-dependent production of oxaloacetate and has important roles in gluconeogenesis, lipogenesis, insulin secretion and other cellular processes. PC contains the biotin carboxylase (BC), carboxyltransferase (CT) and biotin-carboxyl carrier protein (BCCP) domains. We report here the crystal structures at 2.8-A resolution of full-length PC from Staphylococcus aureus and the C-terminal region (missing only the BC domain) of human PC. A conserved tetrameric association is observed for both enzymes, and our structural and mutagenesis studies reveal a previously uncharacterized domain, the PC tetramerization (PT) domain, which is important for oligomerization. A BCCP domain is located in the active site of the CT domain, providing the first molecular insights into how biotin participates in the carboxyltransfer reaction. There are dramatic differences in domain positions in the monomer and the organization of the tetramer between these enzymes and the PC from Rhizobium etli.

PubMed: 18297087
DOI: 10.1038/nsmb.1393

実験手法

X-RAY DIFFRACTION (2.8 Å)