2bfe

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[[Image:2bfe.png|left|200px]]
[[Image:2bfe.png|left|200px]]
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{{STRUCTURE_2bfe| PDB=2bfe | SCENE= }}
{{STRUCTURE_2bfe| PDB=2bfe | SCENE= }}
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===REACTIVITY MODULATION OF HUMAN BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE BY AN INTERNAL MOLECULAR SWITCH===
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===Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch===
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{{ABSTRACT_PUBMED_16472748}}
 
==About this Structure==
==About this Structure==

Revision as of 07:02, 14 November 2012

Template:STRUCTURE 2bfe

Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch

About this Structure

2bfe is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Machius M, Wynn RM, Chuang JL, Li J, Kluger R, Yu D, Tomchick DR, Brautigam CA, Chuang DT. A versatile conformational switch regulates reactivity in human branched-chain alpha-ketoacid dehydrogenase. Structure. 2006 Feb;14(2):287-98. PMID:16472748 doi:10.1016/j.str.2005.10.009
  • Li J, Wynn RM, Machius M, Chuang JL, Karthikeyan S, Tomchick DR, Chuang DT. Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain alpha-keto acid decarboxylase/dehydrogenase. J Biol Chem. 2004 Jul 30;279(31):32968-78. Epub 2004 May 27. PMID:15166214 doi:http://dx.doi.org/10.1074/jbc.M403611200
  • Wynn RM, Machius M, Chuang JL, Li J, Tomchick DR, Chuang DT. Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase: refined phosphorylation loop structure in the active site. J Biol Chem. 2003 Oct 31;278(44):43402-10. Epub 2003 Aug 5. PMID:12902323 doi:http://dx.doi.org/10.1074/jbc.M306204200
  • Wynn RM, Ho R, Chuang JL, Chuang DT. Roles of active site and novel K+ ion-binding site residues in human mitochondrial branched-chain alpha-ketoacid decarboxylase/dehydrogenase. J Biol Chem. 2001 Feb 9;276(6):4168-74. Epub 2000 Nov 7. PMID:11069910 doi:10.1074/jbc.M008038200

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