3b8k
From Proteopedia
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'''Structure of the Truncated Human Dihydrolipoyl Acetyltransferase (E2)''' | '''Structure of the Truncated Human Dihydrolipoyl Acetyltransferase (E2)''' | ||
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[[Category: Yu, X.]] | [[Category: Yu, X.]] | ||
[[Category: Zhou, Z H.]] | [[Category: Zhou, Z H.]] | ||
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- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:31:13 2008'' | |
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Revision as of 17:31, 4 May 2008
Structure of the Truncated Human Dihydrolipoyl Acetyltransferase (E2)
Overview
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.
About this Structure
3B8K is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structures of the human pyruvate dehydrogenase complex cores: a highly conserved catalytic center with flexible N-terminal domains., Yu X, Hiromasa Y, Tsen H, Stoops JK, Roche TE, Zhou ZH, Structure. 2008 Jan;16(1):104-14. PMID:18184588 Page seeded by OCA on Sun May 4 20:31:13 2008