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1xdj

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(New page: 200px<br /><applet load="1xdj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xdj, resolution 2.20&Aring;" /> '''Crystal Structure of...)
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[[Image:1xdj.gif|left|200px]]<br /><applet load="1xdj" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1xdj, resolution 2.20&Aring;" />
 
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'''Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ and Homocysteine'''<br />
 
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==Overview==
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==Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ and Homocysteine==
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Cobalamin-independent methionine synthase (MetE) catalyzes the transfer of, a methyl group from methyltetrahydrofolate to L-homocysteine (Hcy) without, using an intermediate methyl carrier. Although MetE displays no detectable, sequence homology with cobalamin-dependent methionine synthase (MetH), both enzymes require zinc for activation and binding of Hcy., Crystallographic analyses of MetE from T. maritima reveal an unusual, dual-barrel structure in which the active site lies between the tops of, the two (betaalpha)(8) barrels. The fold of the N-terminal barrel confirms, that it has evolved from the C-terminal polypeptide by gene duplication;, comparisons of the barrels provide an intriguing example of homologous, domain evolution in which binding sites are obliterated. The C-terminal, barrel incorporates the zinc ion that binds and activates Hcy. The, zinc-binding site in MetE is distinguished from the (Cys)(3)Zn site in the, related enzymes, MetH and betaine-homocysteine methyltransferase, by its, position in the barrel and by the metal ligands, which are histidine, cysteine, glutamate, and cysteine in the resting form of MetE. Hcy, associates at the face of the metal opposite glutamate, which moves away, from the zinc in the binary E.Hcy complex. The folate substrate is not, intimately associated with the N-terminal barrel; instead, elements from, both barrels contribute binding determinants in a binary complex in which, the folate substrate is incorrectly oriented for methyl transfer. Atypical, locations of the Hcy and folate sites in the C-terminal barrel presumably, permit direct interaction of the substrates in a ternary complex., Structures of the binary substrate complexes imply that rearrangement of, folate, perhaps accompanied by domain rearrangement, must occur before, formation of a ternary complex that is competent for methyl transfer.
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<StructureSection load='1xdj' size='340' side='right'caption='[[1xdj]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1xdj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XDJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XDJ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>, <scene name='pdbligand=MRY:MESO-ERYTHRITOL'>MRY</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xdj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xdj OCA], [https://pdbe.org/1xdj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xdj RCSB], [https://www.ebi.ac.uk/pdbsum/1xdj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xdj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/METE_THEMA METE_THEMA] Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation (By similarity).
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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/xd/1xdj_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/main_output.php?pdb_ID=1xdj ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1XDJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with SO4, ZN, HCS and MRY as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XDJ OCA].
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*[[Methionine synthase 3D structures|Methionine synthase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication., Pejchal R, Ludwig ML, PLoS Biol. 2005 Feb;3(2):e31. Epub 2004 Dec 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15630480 15630480]
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[[Category: Large Structures]]
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[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
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[[Category: Single protein]]
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Ludwig, M.L.]]
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[[Category: Ludwig ML]]
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[[Category: Pejchal, R.]]
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[[Category: Pejchal R]]
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[[Category: HCS]]
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[[Category: MRY]]
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[[Category: SO4]]
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[[Category: ZN]]
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[[Category: homocysteine]]
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[[Category: methyltetrahydrofolate]]
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[[Category: tim barrel]]
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[[Category: zinc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:00:22 2007''
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Current revision

Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ and Homocysteine

PDB ID 1xdj

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