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| - | ==METHYLTRANSFERASE NATIVE== | + | |
| - | <StructureSection load='2yci' size='340' side='right' caption='[[2yci]], [[Resolution|resolution]] 1.78Å' scene=''> | + | ==methyltransferase native== |
| | + | <StructureSection load='2yci' size='340' side='right'caption='[[2yci]], [[Resolution|resolution]] 1.78Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2yci]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans Carboxydothermus hydrogenoformans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YCI OCA]. <br> | + | <table><tr><td colspan='2'>[[2yci]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans_Z-2901 Carboxydothermus hydrogenoformans Z-2901]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YCI FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><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]] 1.78Å</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yck|2yck]], [[2ycj|2ycj]], [[2ycl|2ycl]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=2yci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yci OCA], [https://pdbe.org/2yci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yci RCSB], [https://www.ebi.ac.uk/pdbsum/2yci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yci ProSAT]</span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yci OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yci RCSB], [http://www.ebi.ac.uk/pdbsum/2yci PDBsum]</span></td></tr> | + | </table> |
| - | <table> | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q3ACR9_CARHZ Q3ACR9_CARHZ] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | Structural Basis for Electron and Methyl-Group Transfer in a Methyltransferase System Operating in the Reductive Acetyl-CoA Pathway.,Goetzl S, Jeoung JH, Hennig SE, Dobbek H J Mol Biol. 2011 Aug 5;411(1):96-109. Epub 2011 May 27. PMID:21640123<ref>PMID:21640123</ref> | | Structural Basis for Electron and Methyl-Group Transfer in a Methyltransferase System Operating in the Reductive Acetyl-CoA Pathway.,Goetzl S, Jeoung JH, Hennig SE, Dobbek H J Mol Biol. 2011 Aug 5;411(1):96-109. Epub 2011 May 27. PMID:21640123<ref>PMID:21640123</ref> |
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2yci" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Carboxydothermus hydrogenoformans]] | + | [[Category: Carboxydothermus hydrogenoformans Z-2901]] |
| - | [[Category: Dobbek, H.]] | + | [[Category: Large Structures]] |
| - | [[Category: Goetzl, S.]] | + | [[Category: Dobbek H]] |
| - | [[Category: Hennig, S E.]] | + | [[Category: Goetzl S]] |
| - | [[Category: Jeoung, J H.]] | + | [[Category: Hennig SE]] |
| - | [[Category: Transferase]] | + | [[Category: Jeoung JH]] |
| Structural highlights
Function
Q3ACR9_CARHZ
Publication Abstract from PubMed
Several anaerobic acetogenic, methanogenic, hydrogenogenic, and sulfate-reducing microorganisms are able to use the reductive acetyl-CoA (Wood-Ljungdahl) pathway to convert CO(2) into biomass. The reductive acetyl-CoA pathway consists of two branches connected by the Co/Fe-containing corrinoid iron-sulfur protein (CoFeSP), which transfers a methyl group from a methyltransferase (MeTr)/methyltetrahydrofolate (CH(3)-H(4) folate) complex to the reduced Ni-Ni-[4Fe-4S] cluster (cluster A) of acetyl-CoA synthase. We investigated the CoFeSP and MeTr couple of the hydrogenogenic bacterium Carboxydothermus hydrogenoformans and show that the two proteins are able to catalyze the methyl-group transfer reaction from CH(3)-H(4) folate to the Co(I) center of CoFeSP. We determined the crystal structures of both proteins. The structure of CoFeSP includes the previously unresolved N-terminal domain of the large subunit of CoFeSP, revealing a unique four-helix-bundle-like architecture in which a [4Fe-4S] cluster is shielded by hydrophobic amino acids. It further reveals that the corrinoid and the [4Fe-4S] cluster binding domains are mobile, which is mandatory for the postulated electron transfer between them. Furthermore, we solved the crystal structures of apo-MeTr, CH(3)-H(4)-folate-bound MeTr, and H(4)-folate-bound MeTr, revealing a substrate-induced closure of the CH(3)-H(4) folate binding cavity of MeTr. We observed three different conformations of Asn200 depending on the substrate bound in the active site, demonstrating its conformational modulation by hydrogen-bonding interactions with the substrate. The observed flexibility could be essential to stabilize the transition state during methyl-group transfer. The conformational space and role of Asn200 are likely conserved in homologous cobalamin-dependent MeTrs such as methionine synthase.
Structural Basis for Electron and Methyl-Group Transfer in a Methyltransferase System Operating in the Reductive Acetyl-CoA Pathway.,Goetzl S, Jeoung JH, Hennig SE, Dobbek H J Mol Biol. 2011 Aug 5;411(1):96-109. Epub 2011 May 27. PMID:21640123[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Goetzl S, Jeoung JH, Hennig SE, Dobbek H. Structural Basis for Electron and Methyl-Group Transfer in a Methyltransferase System Operating in the Reductive Acetyl-CoA Pathway. J Mol Biol. 2011 Aug 5;411(1):96-109. Epub 2011 May 27. PMID:21640123 doi:10.1016/j.jmb.2011.05.025
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