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TitleCryo-EM analysis reveals new insights into the mechanism of action of pyruvate carboxylase.
Journal, issue, pagesStructure, Vol. 18, Issue 10, Page 1300-1310, Year 2010
Publish dateOct 13, 2010
AuthorsGorka Lasso / Linda P C Yu / David Gil / Song Xiang / Liang Tong / Mikel Valle /
PubMed AbstractPyruvate 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 ...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.
External linksStructure / PubMed:20947019 / PubMed Central
MethodsEM (single particle)
Resolution7.9 - 13.4 Å
Structure data

EMDB-1736:
Pyruvate carboxylase from S. aureus after addition of Acetyl-CoA
Method: EM (single particle) / Resolution: 13.4 Å

EMDB-1737:
Pyruvate carboxylase from S. aureus after addition of acetyl-CoA, AMP-PNP, KHCO3 and pyruvate
Method: EM (single particle) / Resolution: 13.2 Å

EMDB-1738:
Pyruvate carboxylase from S. aureus after addition of acetyl-CoA and AMP-PNP
Method: EM (single particle) / Resolution: 12.3 Å

EMDB-1741:
Pyruvate carboxylase from S. aureus after addition of acetyl-CoA, AMP-PNP, KHCO3 and oxaloacetate (total map prior to maximum likekihood based classification)
Method: EM (single particle) / Resolution: 7.9 Å

EMDB-1742:
Pyruvate carboxylase from S. aureus after addition of acetyl-Coa, AMP-PNP, KHCO3 and oxaloacetate (based on a subset obtained after maximum likelihood based classification)
Method: EM (single particle) / Resolution: 9.1 Å

EMDB-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)
Method: EM (single particle) / Resolution: 9.5 Å

EMDB-1744:
Pyruvate carboxylase from S. aureus after addition of acetyl-CoA, AMP-PNP, KHCO3 and oxaloacetate (based on a subset obtained after maximum likelihood based classification)
Method: EM (single particle) / Resolution: 8.5 Å

Source
  • Staphylococcus aureus (bacteria)

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