3b8k
From Proteopedia
(New page: 200px<br /><applet load="3b8k" size="350" color="white" frame="true" align="right" spinBox="true" caption="3b8k" /> '''Structure of the Truncated Human Dihydrolipo...) |
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==Overview== | ==Overview== | ||
| - | Dihydrolipoyl acetyltransferase (E2) is the central component of pyruvate | + | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hiromasa, Y.]] | [[Category: Hiromasa, Y.]] | ||
| - | [[Category: Roche, T | + | [[Category: Roche, T E.]] |
| - | [[Category: Stoops, J | + | [[Category: Stoops, J K.]] |
[[Category: Tsen, H.]] | [[Category: Tsen, H.]] | ||
[[Category: Yu, X.]] | [[Category: Yu, X.]] | ||
| - | [[Category: Zhou, Z | + | [[Category: Zhou, Z H.]] |
[[Category: central beta-sheet surrounded by five alpha-helices]] | [[Category: central beta-sheet surrounded by five alpha-helices]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:04:09 2008'' |
Revision as of 17:04, 21 February 2008
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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. Active as Dihydrolipoyllysine-residue acetyltransferase, with EC number 2.3.1.12 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
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