7xcm
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of sulfite MttB structure at 3.2 A resolution== | |
| + | <StructureSection load='7xcm' size='340' side='right'caption='[[7xcm]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7xcm]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_barkeri_MS Methanosarcina barkeri MS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XCM FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BG3:3-METHYL-5-SULFO-PYRROLIDINE-2-CARBOXYLIC+ACID'>BG3</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=7xcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xcm OCA], [https://pdbe.org/7xcm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xcm RCSB], [https://www.ebi.ac.uk/pdbsum/7xcm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xcm ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MTTB_METBA MTTB_METBA] Catalyzes the transfer of a methyl group from trimethylamine to the corrinoid cofactor of MttC.<ref>PMID:9006042</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The 22nd genetically encoded amino acid, pyrrolysine, plays a unique role in the key step in the growth of methanogens on mono-, di-, and tri-methylamines by activating the methyl group of these substrates for transfer to a corrinoid cofactor. Previous crystal structures of the Methanosarcina barkeri monomethylamine methyltransferase elucidated the structure of pyrrolysine and provide insight into its role in monomethylamine activation. Herein, we report the second structure of a pyrrolysine-containing protein, the M. barkeri trimethylamine methyltransferase MttB, and its structure bound to sulfite, a substrate analog of trimethylamine. We also report the structure of MttB in complex with its cognate corrinoid protein MttC, which specifically receives the methyl group from the pyrrolysine-activated trimethylamine substrate during methanogenesis. Together these structures provide key insights into the role of pyrrolysine in methyl group transfer from trimethylamine to the corrinoid cofactor in MttC. | ||
| - | + | Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex.,Li J, Kang PT, Jiang R, Lee JY, Soares JA, Krzycki JA, Chan MK Commun Biol. 2023 Jan 16;6(1):54. doi: 10.1038/s42003-022-04397-3. PMID:36646841<ref>PMID:36646841</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7xcm" style="background-color:#fffaf0;"></div> |
| - | [[Category: Chan | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Methanosarcina barkeri MS]] | ||
| + | [[Category: Chan MK]] | ||
| + | [[Category: Li J]] | ||
Current revision
Crystal structure of sulfite MttB structure at 3.2 A resolution
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