1EZW

STRUCTURE OF COENZYME F420 DEPENDENT TETRAHYDROMETHANOPTERIN REDUCTASE FROM METHANOPYRUS KANDLERI

Summary for 1EZW

• Entry DOI: 10.2210/pdb1ezw/pdb
• Related: 1F07
• Descriptor: COENZYME F420-DEPENDENT N5,N10-METHYLENETETRAHYDROMETHANOPTERIN REDUCTASE, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: (beta, alpha)8 barrel, tim barrel, oxidoreductase
• Biological source: Methanopyrus kandleri
• Cellular location: Cytoplasm: Q8TXY4
• Total number of polymer chains: 1
• Total formula weight: 37610.41

Authors

Shima, S.,Warkentin, E.,Grabarse, W.,Thauer, R.K.,Ermler, U. (deposition date: 2000-05-12, 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 (1.65 Å)