1lua
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(New page: 200px<br /><applet load="1lua" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lua, resolution 1.90Å" /> '''Structure of methyle...)
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Revision as of 18:46, 20 November 2007
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Structure of methylene-tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1 complexed with NADP
Overview
NADP-dependent methylene-H(4)MPT dehydrogenase, MtdA, from, Methylobacterium extorquens AM1 catalyzes the dehydrogenation of, methylene-tetrahydromethanopterin and methylene-tetrahydrofolate with, NADP(+) as cosubstrate. The X-ray structure of MtdA with and without NADP, bound was established at 1.9 A resolution. The enzyme is present as a, homotrimer. The alpha,beta fold of the monomer is related to that of, methylene-H(4)F dehydrogenases, suggesting a common evolutionary origin., The position of the active site is located within a large crevice built up, by the two domains of one subunit and one domain of a second subunit., Methylene-H(4)MPT could be modeled into the cleft, and crucial active site, residues such as Phe18, Lys256, His260, and Thr102 were identified. The, molecular basis of the different substrate specificities and different, catalytic demands of MtdA compared to methylene-H(4)F dehydrogenases are, discussed.
About this Structure
1LUA is a Single protein structure of sequence from Methylobacterium extorquens with NAP as ligand. Active as Methylenetetrahydrofolate dehydrogenase (NADP(+)), with EC number 1.5.1.5 Full crystallographic information is available from OCA.
Reference
Structure of methylene-tetrahydromethanopterin dehydrogenase from methylobacterium extorquens AM1., Ermler U, Hagemeier CH, Roth A, Demmer U, Grabarse W, Warkentin E, Vorholt JA, Structure. 2002 Aug;10(8):1127-37. PMID:12176390
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