2qf7

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Revision as of 11:46, 23 January 2008

Image:2qf7.jpg

Crystal structure of a complete multifunctional pyruvate carboxylase from Rhizobium etli

Overview

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.

About this Structure

2QF7 is a Single protein structure of sequence from Rhizobium etli with , , , , , and as ligands. Active as Pyruvate carboxylase, with EC number 6.4.1.1 Full crystallographic information is available from OCA.

Reference

Domain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzyme., St Maurice M, Reinhardt L, Surinya KH, Attwood PV, Wallace JC, Cleland WW, Rayment I, Science. 2007 Aug 24;317(5841):1076-9. PMID:17717183

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