2a8x
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(New page: 200px<br /><applet load="2a8x" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a8x, resolution 2.40Å" /> '''Crystal Structure of...)
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Revision as of 05:52, 21 November 2007
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Crystal Structure of Lipoamide Dehydrogenase from Mycobacterium tuberculosis
Overview
We report the 2.4 A crystal structure for lipoamide dehydrogenase encoded, by lpdC from Mycobacterium tuberculosis. Based on the Lpd structure and, sequence alignment between bacterial and eukaryotic Lpd sequences, we, generated single point mutations in Lpd and assayed the resulting proteins, for their ability to catalyze lipoamide reduction/oxidation alone and in, complex with other proteins that participate in pyruvate dehydrogenase and, peroxidase activities. The results suggest that amino acid residues, conserved in mycobacterial species but not conserved in eukaryotic Lpd, family members modulate either or both activities and include Arg-93, His-98, Lys-103, and His-386. In addition, Arg-93 and His-386 are involved, in forming both "open" and "closed" active site conformations, suggesting, that these residues play a role in dynamically regulating Lpd function., Taken together, these data suggest protein surfaces that should be, considered while developing strategies for inhibiting this enzyme.
About this Structure
2A8X is a Single protein structure of sequence from Mycobacterium tuberculosis with FAD and MPD as ligands. Active as Dihydrolipoyl dehydrogenase, with EC number 1.8.1.4 Full crystallographic information is available from OCA.
Reference
Crystal structure and functional analysis of lipoamide dehydrogenase from Mycobacterium tuberculosis., Rajashankar KR, Bryk R, Kniewel R, Buglino JA, Nathan CF, Lima CD, J Biol Chem. 2005 Oct 7;280(40):33977-83. Epub 2005 Aug 10. PMID:16093239
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