3b8k
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span> |
|GENE= DLAT, DLTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= DLAT, DLTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1eaa|1EAA]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b8k OCA], [http://www.ebi.ac.uk/pdbsum/3b8k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3b8k RCSB]</span> | ||
}} | }} | ||
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[[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 Mon Mar 31 05:24:10 2008'' |
Revision as of 02:24, 31 March 2008
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| Gene: | DLAT, DLTA (Homo sapiens) | ||||||
| Activity: | Dihydrolipoyllysine-residue acetyltransferase, with EC number 2.3.1.12 | ||||||
| Related: | 1EAA
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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