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| | <StructureSection load='5l8x' size='340' side='right'caption='[[5l8x]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='5l8x' size='340' side='right'caption='[[5l8x]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5l8x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Metja Metja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L8X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5L8X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5l8x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L8X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMR:(2S)-2-HYDROXYBUTANEDIOIC+ACID'>LMR</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mtrA, MJ0851 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 METJA])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMR:(2S)-2-HYDROXYBUTANEDIOIC+ACID'>LMR</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tetrahydromethanopterin_S-methyltransferase Tetrahydromethanopterin S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.86 2.1.1.86] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5l8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l8x OCA], [https://pdbe.org/5l8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l8x RCSB], [https://www.ebi.ac.uk/pdbsum/5l8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l8x ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5l8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l8x OCA], [http://pdbe.org/5l8x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l8x RCSB], [http://www.ebi.ac.uk/pdbsum/5l8x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l8x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MTRA_METJA MTRA_METJA]] Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.[HAMAP-Rule:MF_01093] | + | [https://www.uniprot.org/uniprot/MTRA_METJA MTRA_METJA] Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.[HAMAP-Rule:MF_01093] |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | In the three domains of life, vitamin B12 (cobalamin) is primarily used in methyltransferase and isomerase reactions. The methyltransferase complex MtrA-H of methanogenic archaea has a key function in energy conservation by catalysing the methyl transfer from methyl-tetrahydromethanopterin to coenzyme M and its coupling with sodium-ion translocation. The cobalamin-binding subunit MtrA is not homologous to any known B12-binding proteins and is proposed as the motor of the sodium-ion pump. Here, we present crystal structures of the soluble domain of the membrane-associated MtrA from Methanocaldococcus jannaschii and the cytoplasmic MtrA homologue/cobalamin complex from Methanothermus fervidus. The MtrA fold corresponds to the Rossmann-type alpha/beta fold, which is also found in many cobalamin-containing proteins. Surprisingly, the cobalamin-binding site of MtrA differed greatly from all the other cobalamin-binding sites. Nevertheless, the hydrogen-bond linkage at the lower axial-ligand site of cobalt was equivalently constructed to that found in other methyltransferases and mutases. A distinct polypeptide segment fixed through the hydrogen-bond linkage in the relaxed Co(III) state might be involved in propagating the energy released upon corrinoid demethylation to the sodium-translocation site by a conformational change.
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| - | MtrA of the sodium ion pumping methyltransferase binds cobalamin in a unique mode.,Wagner T, Ermler U, Shima S Sci Rep. 2016 Jun 21;6:28226. doi: 10.1038/srep28226. PMID:27324530<ref>PMID:27324530</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5l8x" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Metja]] | + | [[Category: Methanocaldococcus jannaschii DSM 2661]] |
| - | [[Category: Tetrahydromethanopterin S-methyltransferase]]
| + | [[Category: Ermler U]] |
| - | [[Category: Ermler, U]] | + | [[Category: Shima S]] |
| - | [[Category: Shima, S]] | + | [[Category: Wagner T]] |
| - | [[Category: Wagner, T]] | + | |
| - | [[Category: Cobalamin]]
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| - | [[Category: Coenzymem]]
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| - | [[Category: Hyperthermophile]]
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| - | [[Category: Marine organism]]
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| - | [[Category: Membrane protein]]
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| - | [[Category: Methanogenesis]]
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| - | [[Category: Methyltransferase]]
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| - | [[Category: Motor pump]]
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| - | [[Category: Rossmann fold]]
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| - | [[Category: Transferase]]
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| - | [[Category: Vitamin b12]]
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