2i2x: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2i2x]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_barkeri Methanosarcina barkeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I2X FirstGlance]. <br>
<table><tr><td colspan='2'>[[2i2x]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_barkeri Methanosarcina barkeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I2X FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B13:5-HYDROXYBENZIMIDAZOLYLCOB(III)AMIDE'>B13</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 2.5&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methanol--corrinoid_protein_Co-methyltransferase Methanol--corrinoid protein Co-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.90 2.1.1.90] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B13:5-HYDROXYBENZIMIDAZOLYLCOB(III)AMIDE'>B13</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2i2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i2x OCA], [https://pdbe.org/2i2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i2x RCSB], [https://www.ebi.ac.uk/pdbsum/2i2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i2x 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=2i2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i2x OCA], [https://pdbe.org/2i2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i2x RCSB], [https://www.ebi.ac.uk/pdbsum/2i2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i2x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/MTAB_METBF MTAB_METBF]] Methyltransferase involved in methanogenesis in the methanol pathway. Catalyzes the methylation of the MtaC-bound cob(I)amide.<ref>PMID:9057830</ref> <ref>PMID:9363780</ref> [[https://www.uniprot.org/uniprot/MTAC_METBF MTAC_METBF]] Harbors a corrinoid prosthetic group and acts as a methyl group carrier in methanogenesis in the methanol pathway. The methyl group of methanol is first transferred to the corrinoid prosthetic group of MtaC in the cob(I)amide oxidation state. This reaction is mediated by MtaB. The methyl group from MtaC is then transferred to coenzyme M by MtaA.<ref>PMID:9057830</ref> 
[https://www.uniprot.org/uniprot/MTAB_METBF MTAB_METBF] Methyltransferase involved in methanogenesis in the methanol pathway. Catalyzes the methylation of the MtaC-bound cob(I)amide.<ref>PMID:9057830</ref> <ref>PMID:9363780</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=2i2x ConSurf].
</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=2i2x ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Some methanogenic and acetogenic microorganisms have the catalytic capability to cleave heterolytically the C O bond of methanol. To obtain insight into the elusive enzymatic mechanism of this challenging chemical reaction we have investigated the methanol-activating MtaBC complex from Methanosarcina barkeri composed of the zinc-containing MtaB and the 5-hydroxybenzimidazolylcobamide-carrying MtaC subunits. Here we report the 2.5-A crystal structure of this complex organized as a (MtaBC)(2) heterotetramer. MtaB folds as a TIM barrel and contains a novel zinc-binding motif. Zinc(II) lies at the bottom of a funnel formed at the C-terminal beta-barrel end and ligates to two cysteinyl sulfurs (Cys-220 and Cys-269) and one carboxylate oxygen (Glu-164). MtaC is structurally related to the cobalamin-binding domain of methionine synthase. Its corrinoid cofactor at the top of the Rossmann domain reaches deeply into the funnel of MtaB, defining a region between zinc(II) and the corrinoid cobalt that must be the binding site for methanol. The active site geometry supports a S(N)2 reaction mechanism, in which the C O bond in methanol is activated by the strong electrophile zinc(II) and cleaved because of an attack of the supernucleophile cob(I)amide. The environment of zinc(II) is characterized by an acidic cluster that increases the charge density on the zinc(II), polarizes methanol, and disfavors deprotonation of the methanol hydroxyl group. Implications of the MtaBC structure for the second step of the reaction, in which the methyl group is transferred to coenzyme M, are discussed.
Insight into the mechanism of biological methanol activation based on the crystal structure of the methanol-cobalamin methyltransferase complex.,Hagemeier CH, Krer M, Thauer RK, Warkentin E, Ermler U Proc Natl Acad Sci U S A. 2006 Dec 12;103(50):18917-22. Epub 2006 Dec 1. PMID:17142327<ref>PMID:17142327</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2i2x" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Methanol--corrinoid protein Co-methyltransferase]]
[[Category: Methanosarcina barkeri]]
[[Category: Methanosarcina barkeri]]
[[Category: Ermler, U]]
[[Category: Ermler U]]
[[Category: Hagemeier, C H]]
[[Category: Hagemeier CH]]
[[Category: Kruer, M]]
[[Category: Kruer M]]
[[Category: Thauer, R K]]
[[Category: Thauer RK]]
[[Category: Warkentin, E]]
[[Category: Warkentin E]]
[[Category: Transferase]]

Revision as of 09:01, 21 February 2024

Crystal structure of methanol:cobalamin methyltransferase complex MtaBC from Methanosarcina barkeri

2i2x, resolution 2.50Å

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