1F07

STRUCTURE OF COENZYME F420 DEPENDENT TETRAHYDROMETHANOPTERIN REDUCTASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM

Summary for 1F07

• Entry DOI: 10.2210/pdb1f07/pdb
• Related: 1EZW
• Descriptor: COENZYME F420-DEPENDENT N5,N10-METHYLENETETRAHYDROMETHANOPTERIN REDUCTASE, 3[N-MORPHOLINO]PROPANE SULFONIC ACID, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (5 entities in total)
• Functional Keywords: (beta, alpha)8 barrel, tim barrel, oxidoreductase
• Biological source: Methanothermobacter thermautotrophicus
• Total number of polymer chains: 4
• Total formula weight: 135453.95

Authors

Shima, S.,Warkentin, E.,Grabarse, W.,Thauer, R.K.,Ermler, U. (deposition date: 2000-05-15, release date: 2000-09-06, Last modification date: 2024-02-07)

Primary citation

Shima, S.,Warkentin, E.,Grabarse, W.,Sordel, M.,Wicke, M.,Thauer, R.K.,Ermler, U.
Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea.
J.Mol.Biol., 300:935-950, 2000

PubMed Abstract: 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.

PubMed: 10891279
DOI: 10.1006/jmbi.2000.3909

Experimental method

X-RAY DIFFRACTION (2 Å)