3BG3: Crystal Structure Of Human Pyruvate Carboxylase (missing The Biotin Carboxylase Domain At The N-terminus)

Citation:
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.
PDB ID: 3BG3Download
MMDB ID: 62719
PDB Deposition Date: 2007/11/26
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.8  Å
Source Organism:
Similar Structures:
Biological Unit for 3BG3: tetrameric; determined by author and by software (PISA)
Molecular Components in 3BG3
Label Count Molecule
Proteins (4 molecules)
4
Pyruvate Carboxylase, Mitochondrial(Gene symbol: PC)
Molecule annotation
Chemicals (9 molecules)
1
4
2
4
3
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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