EMD-1743

Single-particle
9.5 Å
EMD-1743 Deposition: 02/06/2010
Map released: 20/05/2011
Last modified: 20/05/2011
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-1743

Pyruvate carboxylase from S. aureus after addition of actyl-CoA, AMP-PNP, KHCO3 and oxaloacetate (based on a subset obtained after maximum likelihood based classification)

EMD-1743

Single-particle
9.5 Å
EMD-1743 Deposition: 02/06/2010
Map released: 20/05/2011
Last modified: 20/05/2011
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Staphylococcus aureus
Sample: Pyruvate carboxylase from S. aureus after addition of actyl-CoA, AMP-PNP, KHCO3 and oxaloacetate (based on a subset obtyained after maximum likelihood based classification)

Deposition Authors: Lasso G, Yu LPC, Gil D , Xiang S , Tong L , Valle M
Cryo-EM analysis reveals new insights into the mechanism of action of pyruvate carboxylase.
Lasso G, Yu LP, Gil D , Xiang S , Tong L , Valle M
(2010) Structure , 18 , 1300 - 1310
Abstract:
Pyruvate carboxylase (PC) is a conserved multifunctional enzyme linked to important metabolic diseases. PC homotetramer is arranged in two layers with two opposing monomers per layer. Cryo-EM explores the conformational variability of PC in the presence of different substrates. The results demonstrate that the biotin-carboxyl carrier protein (BCCP) domain localizes near the biotin carboxylase (BC) domain of its own monomer and travels to the carboxyltransferase (CT) domain of the opposite monomer. All density maps show noticeable conformational differences between layers, mainly for the BCCP and BC domains. This asymmetry may be indicative of a coordination mechanism where monomers from different layers catalyze the BC and CT reactions consecutively. A conformational change of the PC tetramerization (PT) domain suggests a new functional role in communication. A long-range communication pathway between subunits in different layers, via interacting PT-PT and BC-BC domains, may be responsible for the cooperativity of PC from Staphylococcus aureus.