1z69

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[[Image:1z69.png|left|200px]]
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==Crystal structure of methylenetetrahydromethanopterin reductase (Mer) in complex with coenzyme F420==
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<StructureSection load='1z69' size='340' side='right' caption='[[1z69]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1z69]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanosarcina_barkeri Methanosarcina barkeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z69 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z69 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PG:2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>1PG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F42:COENZYME+F420'>F42</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ezw|1ezw]], [[1f07|1f07]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5,10-methylenetetrahydromethanopterin_reductase 5,10-methylenetetrahydromethanopterin reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.99.11 1.5.99.11] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z69 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1z69 RCSB], [http://www.ebi.ac.uk/pdbsum/1z69 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z6/1z69_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Methylenetetratetrahydromethanopterin reductase (Mer) is involved in CO(2) reduction to methane in methanogenic archaea and catalyses the reversible reduction of methylenetetrahydromethanopterin (methylene-H(4)MPT) to methyl-H(4)MPT with coenzyme F(420)H(2), which is a reduced 5'-deazaflavin. Mer was recently established as a TIM barrel structure containing a nonprolyl cis-peptide bond but the binding site of the substrates remained elusive. We report here on the crystal structure of Mer in complex with F(420) at 2.6 A resolution. The isoalloxazine ring is present in a pronounced butterfly conformation, being induced from the Re-face of F(420) by a bulge that contains the non-prolyl cis-peptide bond. The bindingmode of F(420) is very similar to that in F(420)-dependent alcohol dehydrogenase Adf despite the low sequence identity of 21%. Moreover, binding of F(420) to the apoenzyme was only associated with minor conformational changes of the polypeptide chain. These findings allowed us to build an improved model of FMN into its binding site in bacterial luciferase, which belongs to the same structural family as Mer and Adf and also contains a nonprolyl cis-peptide bond in an equivalent position.
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{{STRUCTURE_1z69| PDB=1z69 | SCENE= }}
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Crystal structure of methylenetetrahydromethanopterin reductase (Mer) in complex with coenzyme F420: Architecture of the F420/FMN binding site of enzymes within the nonprolyl cis-peptide containing bacterial luciferase family.,Aufhammer SW, Warkentin E, Ermler U, Hagemeier CH, Thauer RK, Shima S Protein Sci. 2005 Jul;14(7):1840-9. Epub 2005 Jun 3. PMID:15937276<ref>PMID:15937276</ref>
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===Crystal structure of methylenetetrahydromethanopterin reductase (Mer) in complex with coenzyme F420===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_15937276}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1z69]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanosarcina_barkeri Methanosarcina barkeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z69 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:015937276</ref><references group="xtra"/>
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[[Category: 5,10-methylenetetrahydromethanopterin reductase]]
[[Category: 5,10-methylenetetrahydromethanopterin reductase]]
[[Category: Methanosarcina barkeri]]
[[Category: Methanosarcina barkeri]]

Revision as of 20:49, 29 September 2014

Crystal structure of methylenetetrahydromethanopterin reductase (Mer) in complex with coenzyme F420

1z69, resolution 2.61Å

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