1f07

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[[Image:1f07.gif|left|200px]]
[[Image:1f07.gif|left|200px]]
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{{Structure
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|PDB= 1f07 |SIZE=350|CAPTION= <scene name='initialview01'>1f07</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1f07", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|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>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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{{STRUCTURE_1f07| PDB=1f07 | SCENE= }}
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|RELATEDENTRY=[[1ezw|1EZW]]
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|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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'''STRUCTURE OF COENZYME F420 DEPENDENT TETRAHYDROMETHANOPTERIN REDUCTASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''
'''STRUCTURE OF COENZYME F420 DEPENDENT TETRAHYDROMETHANOPTERIN REDUCTASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''
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[[Category: Thauer, R K.]]
[[Category: Thauer, R K.]]
[[Category: Warkentin, E.]]
[[Category: Warkentin, E.]]
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[[Category: (beta]]
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[[Category: Tim barrel]]
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[[Category: alpha)8 barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:44:06 2008''
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[[Category: tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:13:11 2008''
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Revision as of 12:44, 2 May 2008

Image:1f07.gif

Template:STRUCTURE 1f07

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 Page seeded by OCA on Fri May 2 15:44:06 2008

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