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TitleStructures of the human pyruvate dehydrogenase complex cores: a highly conserved catalytic center with flexible N-terminal domains.
Journal, issue, pagesStructure, Vol. 16, Issue 1, Page 104-114, Year 2008
Publish dateMar 19, 2008
AuthorsXuekui Yu / Yasuaki Hiromasa / Hua Tsen / James K Stoops / Thomas E Roche / Z Hong Zhou /
PubMed AbstractDihydrolipoyl acetyltransferase (E2) is the central component of pyruvate dehydrogenase complex (PDC), which converts pyruvate to acetyl-CoA. Structural comparison by cryo-electron microscopy (cryo- ...Dihydrolipoyl acetyltransferase (E2) is the central component of pyruvate dehydrogenase complex (PDC), which converts pyruvate to acetyl-CoA. Structural comparison by cryo-electron microscopy (cryo-EM) of the human full-length and truncated E2 (tE2) cores revealed flexible linkers emanating from the edges of trimers of the internal catalytic domains. Using the secondary structure constraints revealed in our 8 A cryo-EM reconstruction and the prokaryotic tE2 atomic structure as a template, we derived a pseudo atomic model of human tE2. The active sites are conserved between prokaryotic tE2 and human tE2. However, marked structural differences are apparent in the hairpin domain and in the N-terminal helix connected to the flexible linker. These permutations away from the catalytic center likely impart structures needed to integrate a second component into the inner core and provide a sturdy base for the linker that holds the pyruvate dehydrogenase for access by the E2-bound regulatory kinase/phosphatase components in humans.
External linksStructure / PubMed:18184588 / PubMed Central
MethodsEM (single particle)
Resolution8.8 Å
Structure data

1448

3b8k

EMDB-1448: Structures of the human pyruvate dehydrogenase complex cores: a highly conserved catalytic center with flexible N-terminal domains.
PDB-3b8k: Structure of the Truncated Human Dihydrolipoyl Acetyltransferase (E2)
Method: EM (single particle) / Resolution: 8.8 Å

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / central beta-sheet surrounded by five alpha-helices

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