1k8m: Difference between revisions

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[[Image:1k8m.jpg|left|200px]]
[[Image:1k8m.jpg|left|200px]]


{{Structure
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{{STRUCTURE_1k8m| PDB=1k8m  | SCENE= }}  
|RELATEDENTRY=[[1k8o|1K8O]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k8m OCA], [http://www.ebi.ac.uk/pdbsum/1k8m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k8m RCSB]</span>
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'''Solution Structure of the Lipoic Acid-Bearing Domain of the E2 component of Human, Mitochondrial Branched-Chain alpha-Ketoacid Dehydrogenase'''
'''Solution Structure of the Lipoic Acid-Bearing Domain of the E2 component of Human, Mitochondrial Branched-Chain alpha-Ketoacid Dehydrogenase'''
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[[Category: Chuang, J L.]]
[[Category: Chuang, J L.]]
[[Category: Huang, T h.]]
[[Category: Huang, T h.]]
[[Category: average structure]]
[[Category: Average structure]]
[[Category: experimental nmr data]]
[[Category: Experimental nmr data]]
[[Category: human bckd]]
[[Category: Human bckd]]
[[Category: lipoyl acid bearing]]
[[Category: Lipoyl acid bearing]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:26:20 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:44:54 2008''

Revision as of 22:26, 2 May 2008

File:1k8m.jpg

Template:STRUCTURE 1k8m

Solution Structure of the Lipoic Acid-Bearing Domain of the E2 component of Human, Mitochondrial Branched-Chain alpha-Ketoacid Dehydrogenase


OverviewOverview

The lipoyl-bearing domain (LBD) of the transacylase (E2) subunit of the branched-chain alpha-keto acid dehydrogenase complex plays a central role in substrate channeling in this mitochondrial multienzyme complex. We have employed multidimensional heteronuclear NMR techniques to determine the structure and dynamics of the LBD of the human branched-chain alpha-keto acid dehydrogenase complex (hbLBD). Similar to LBD from other members of the alpha-keto acid dehydrogenase family, the solution structure of hbLBD is a flattened beta-barrel formed by two four-stranded antiparallel beta-sheets. The lipoyl Lys(44) residue resides at the tip of a beta-hairpin comprising a sharp type I beta-turn and the two connecting beta-strands 4 and 5. A prominent V-shaped groove formed by a surface loop, L1, connecting beta 1- and beta 2-strands and the lipoyl lysine beta-hairpin constitutes the functional pocket. We further applied reduced spectral density functions formalism to extract dynamic information of hbLBD from (15)N-T(1), (15)N-T(2), and ((1)H-(15)N) nuclear Overhauser effect data obtained at 600 MHz. The results showed that residues surrounding the lipoyl lysine region comprising the L1 loop and the Lys(44) beta-turn are highly flexible, whereas beta-sheet S1 appears to display a slow conformational exchange process.

About this StructureAbout this Structure

1K8M is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex., Chang CF, Chou HT, Chuang JL, Chuang DT, Huang TH, J Biol Chem. 2002 May 3;277(18):15865-73. Epub 2002 Feb 11. PMID:11839747 Page seeded by OCA on Fri May 2 22:26:20 2008

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