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| | <StructureSection load='4ay7' size='340' side='right'caption='[[4ay7]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4ay7' size='340' side='right'caption='[[4ay7]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ay7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dsm_2053 Dsm 2053]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AY7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ay7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_mazei Methanosarcina mazei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AY7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.8Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4ay8|4ay8]]</div></td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/[Methyl-Co(III)_methylamine-specific_corrinoid_protein]:coenzyme_M_methyltransferase [Methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.247 2.1.1.247] </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=4ay7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ay7 OCA], [https://pdbe.org/4ay7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ay7 RCSB], [https://www.ebi.ac.uk/pdbsum/4ay7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ay7 ProSAT]</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=4ay7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ay7 OCA], [https://pdbe.org/4ay7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ay7 RCSB], [https://www.ebi.ac.uk/pdbsum/4ay7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ay7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8PXZ6_METMA Q8PXZ6_METMA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dsm 2053]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bayer, P]] | + | [[Category: Methanosarcina mazei]] |
| - | [[Category: Blankenfeld, W]] | + | [[Category: Bayer P]] |
| - | [[Category: Faust, A]] | + | [[Category: Blankenfeld W]] |
| - | [[Category: Hensel, R]] | + | [[Category: Faust A]] |
| - | [[Category: Hoeppner, A]] | + | [[Category: Hensel R]] |
| - | [[Category: Rueppel, A]] | + | [[Category: Hoeppner A]] |
| - | [[Category: Thomas, F]] | + | [[Category: Rueppel A]] |
| - | [[Category: Tim barrel]]
| + | [[Category: Thomas F]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q8PXZ6_METMA
Publication Abstract from PubMed
The zinc-containing corrinoid:coenzyme M methyltransferase MtaA is part of the methanol-coenzyme M-methyltransferase complex of Methanosarcina mazei. The whole complex consists of three subunits: MtaA, MtaB and MtaC. The MtaB-MtaC complex catalyses the cleavage of methanol (bound to MtaB) and the transfer of the methyl group onto the cobalt of cob(I)alamin (bound to MtaC). The MtaA-MtaC complex catalyses methyl transfer from methyl-cob(III)alamin (bound to MtaC) to coenzyme M (bound to MtaA). The crystal structure of the MtaB-MtaC complex from M. barkeri has previously been determined. Here, the crystal structures of MtaA from M. mazei in a substrate-free but Zn(2+)-bound state and in complex with Zn(2+) and coenzyme M (HS-CoM) are reported at resolutions of 1.8 and 2.1 A, respectively. A search for homologous proteins revealed that MtaA exhibits 23% sequence identity to human uroporphyrinogen III decarboxylase, which has also the highest structural similarity (r.m.s.d. of 2.03 A for 306 aligned amino acids). The main structural feature of MtaA is a TIM-barrel-like fold, which is also found in all other zinc enzymes that catalyse thiol-group alkylation. The active site of MtaA is situated at the narrow bottom of a funnel such that the thiolate group of HS-CoM points towards the Zn(2+) ion. The Zn(2+) ion in the active site of MtaA is coordinated tetrahedrally via His240, Cys242 and Cys319. In the substrate-free form the fourth ligand is Glu263. Binding of HS-CoM leads to exchange of the O-ligand of Glu263 for the S-ligand of HS-CoM with inversion of the zinc geometry. The interface between MtaA and MtaC for transfer of the methyl group from MtaC-bound methylcobalamin is most likely to be formed by the core complex of MtaB-MtaC and the N-terminal segment (a long loop containing three alpha-helices and a beta-hairpin) of MtaA, which is not part of the TIM-barrel core structure of MtaA.
Structure of the corrinoid:coenzyme M methyltransferase MtaA from Methanosarcina mazei.,Hoeppner A, Thomas F, Rueppel A, Hensel R, Blankenfeldt W, Bayer P, Faust A Acta Crystallogr D Biol Crystallogr. 2012 Nov;68(Pt 11):1549-57. doi:, 10.1107/S090744491203853X. Epub 2012 Oct 18. PMID:23090404[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hoeppner A, Thomas F, Rueppel A, Hensel R, Blankenfeldt W, Bayer P, Faust A. Structure of the corrinoid:coenzyme M methyltransferase MtaA from Methanosarcina mazei. Acta Crystallogr D Biol Crystallogr. 2012 Nov;68(Pt 11):1549-57. doi:, 10.1107/S090744491203853X. Epub 2012 Oct 18. PMID:23090404 doi:http://dx.doi.org/10.1107/S090744491203853X
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