3BG5

Crystal Structure of Staphylococcus Aureus Pyruvate Carboxylase

Summary for 3BG5

• Entry DOI: 10.2210/pdb3bg5/pdb
• Related: 1RQH 3BG3 3BG9
• Descriptor: Pyruvate carboxylase, MANGANESE (II) ION, 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL, ... (5 entities in total)
• Functional Keywords: tim barrel, atp-binding, ligase, nucleotide-binding, pyruvate
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 4
• Total formula weight: 527172.23

Authors

Xiang, S.,Tong, L. (deposition date: 2007-11-26, release date: 2008-02-26, Last modification date: 2023-11-15)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)