2bfe: Difference between revisions

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[[Image:2bfe.png|left|200px]]
[[Image:2bfe.png|left|200px]]


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===REACTIVITY MODULATION OF HUMAN BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE BY AN INTERNAL MOLECULAR SWITCH===
===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

File:2bfe.png

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

  1. 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
  2. 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:https://dx.doi.org/10.1074/jbc.M403611200
  3. 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:https://dx.doi.org/10.1074/jbc.M306204200
  4. 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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