1k8m: Difference between revisions

Revision as of 09:57, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1k8m.png

Template:STRUCTURE 1k8m

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

Template:ABSTRACT PUBMED 11839747

About this StructureAbout this Structure

1K8M is a Single protein structure of sequence from Homo sapiens. Full experimental 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

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 {{STRUCTURE_1k8m|  PDB=1k8m  |  SCENE=  }}
-'''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===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11839747}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11839747 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11839747}}
 ==About this Structure==
-K8M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K8M OCA].
+K8M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K8M OCA].
 ==Reference==
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 [[Category: Human bckd]]
 [[Category: Lipoyl acid bearing]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 09:57:01 2008''