1f07
From Proteopedia
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|PDB= 1f07 |SIZE=350|CAPTION= <scene name='initialview01'>1f07</scene>, resolution 2.00Å | |PDB= 1f07 |SIZE=350|CAPTION= <scene name='initialview01'>1f07</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MPO:3[N-MORPHOLINO]PROPANE+SULFONIC+ACID'>MPO</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ezw|1EZW]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f07 OCA], [http://www.ebi.ac.uk/pdbsum/1f07 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f07 RCSB]</span> | ||
}} | }} | ||
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[[Category: Thauer, R K.]] | [[Category: Thauer, R K.]] | ||
[[Category: Warkentin, E.]] | [[Category: Warkentin, E.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: MPD]] | ||
| - | [[Category: MPO]] | ||
[[Category: (beta]] | [[Category: (beta]] | ||
[[Category: alpha)8 barrel]] | [[Category: alpha)8 barrel]] | ||
[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:13:11 2008'' |
Revision as of 17:13, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1EZW
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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