1f07
From Proteopedia
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STRUCTURE OF COENZYME F420 DEPENDENT TETRAHYDROMETHANOPTERIN REDUCTASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM
Overview
Coenzyme F(420)-dependent methylenetetrahydromethanopterin reductase (Mer), is an enzyme of the Cl metabolism in methanogenic and sulfate reducing, archaea. It is composed of identical 35-40 kDa subunits and lacks a, prosthetic group. The crystal structure of Mer from Methanopyrus kandleri, (kMer) revealed in one crystal form a dimeric and in another a tetrameric, oligomerisation state and that from Methanobacterium thermoautotrophicum, (tMer) a dimeric state. Each monomer is primarily composed of a TIM-barrel, fold enlarged by three insertion regions. Insertion regions 1 and 2, contribute to intersubunit interactions. Insertion regions 2 and 3, together with the C-terminal end of the TIM-barrel core form a cleft where, the binding sites of coenzyme F(420) and methylene-tetrahydromethanopterin, are postulated. Close to the coenzyme F(420)-binding site lies a rarely, observed non-prolyl cis-peptide bond. It is surprising that Mer is, structurally most similar to a bacterial FMN-dependent luciferase which, contains a non-prolyl cis-peptide bond at the equivalent position. The, structure of Mer is also related to that of NADP-dependent FAD-harbouring, methylenetetrahydrofolate reductase (MetF). However, Mer and MetF do not, show sequence similarities although they bind related substrates and, catalyze an analogous reaction.
About this Structure
1F07 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus with CL, MPO and MPD as ligands. Full crystallographic information is available from OCA.
Reference
Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea., Shima S, Warkentin E, Grabarse W, Sordel M, Wicke M, Thauer RK, Ermler U, J Mol Biol. 2000 Jul 21;300(4):935-50. PMID:10891279
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