2QF7

Crystal structure of a complete multifunctional pyruvate carboxylase from Rhizobium etli

Summary for 2QF7

• Entry DOI: 10.2210/pdb2qf7/pdb
• Descriptor: Pyruvate carboxylase protein, MAGNESIUM ION, ZINC ION, ... (9 entities in total)
• Functional Keywords: multi-domain, multi-functional, biotin-dependent, ligase
• Biological source: Rhizobium etli
• Total number of polymer chains: 2
• Total formula weight: 257540.71

Authors

St Maurice, M.,Surinya, K.H.,Rayment, I. (deposition date: 2007-06-27, release date: 2007-09-04, Last modification date: 2025-03-26)

Primary citation

St Maurice, M.,Reinhardt, L.,Surinya, K.H.,Attwood, P.V.,Wallace, J.C.,Cleland, W.W.,Rayment, I.
Domain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzyme
Science, 317:1076-1079, 2007

PubMed Abstract: Biotin-dependent multifunctional enzymes carry out metabolically important carboxyl group transfer reactions and are potential targets for the treatment of obesity and type 2 diabetes. These enzymes use a tethered biotin cofactor to carry an activated carboxyl group between distantly spaced active sites. The mechanism of this transfer has remained poorly understood. Here we report the complete structure of pyruvate carboxylase at 2.0 angstroms resolution, which shows its domain arrangement. The structure, when combined with mutagenic analysis, shows that intermediate transfer occurs between active sites on separate polypeptide chains. In addition, domain rearrangements associated with activator binding decrease the distance between active-site pairs, providing a mechanism for allosteric activation. This description provides insight into the function of biotin-dependent enzymes and presents a new paradigm for multifunctional enzyme catalysis.

PubMed: 17717183
DOI: 10.1126/science.1144504

Experimental method

X-RAY DIFFRACTION (2 Å)