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| | <StructureSection load='1mgt' size='340' side='right'caption='[[1mgt]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='1mgt' size='340' side='right'caption='[[1mgt]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1mgt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_kodakaraensis_(strain_kod1) Pyrococcus kodakaraensis (strain kod1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MGT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1mgt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MGT FirstGlance]. <br> |
| - | </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> | + | </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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methylated-DNA--[protein]-cysteine_S-methyltransferase Methylated-DNA--[protein]-cysteine S-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.63 2.1.1.63] </span></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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mgt OCA], [https://pdbe.org/1mgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mgt RCSB], [https://www.ebi.ac.uk/pdbsum/1mgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mgt 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=1mgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mgt OCA], [https://pdbe.org/1mgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mgt RCSB], [https://www.ebi.ac.uk/pdbsum/1mgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mgt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/OGT_PYRKO OGT_PYRKO]] Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.<ref>PMID:9613574</ref>
| + | [https://www.uniprot.org/uniprot/OGT_THEKO OGT_THEKO] Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.[HAMAP-Rule:MF_00772]<ref>PMID:9613574</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fujiwara, S]] | + | [[Category: Thermococcus kodakarensis KOD1]] |
| - | [[Category: Hashimoto, H]] | + | [[Category: Fujiwara S]] |
| - | [[Category: Imanaka, T]] | + | [[Category: Hashimoto H]] |
| - | [[Category: Inoue, T]] | + | [[Category: Imanaka T]] |
| - | [[Category: Kai, Y]] | + | [[Category: Inoue T]] |
| - | [[Category: Nishioka, M]] | + | [[Category: Kai Y]] |
| - | [[Category: Takagi, M]] | + | [[Category: Nishioka M]] |
| - | [[Category: Dna repair protein]]
| + | [[Category: Takagi M]] |
| - | [[Category: Hyperthermostability]]
| + | |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Suicidal enzyme]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
OGT_THEKO Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.[HAMAP-Rule:MF_00772][1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of O6-methylguanine-DNA methyltransferase (EC 2.1.1.63) of hyperthermophilic archaeon Pyrococcuskodakaraensis strain KOD1 (Pk -MGMT) was determined by single isomorphous replacement method with anomalous scattering (SIRAS) at 1.8 A resolution. The archaeal protein is extremely thermostable and repairs alkylated DNA by suicidal alkyl transfer from guanine O6 to its own cysteine residue. Archaea constitute the third primary kingdom of living organisms, sharing characteristics with procaryotic and eucaryotic cells. They live in various extreme environments and are thought to include the most ancient organisms on the earth. Structural studies on hyperthermophilic archaeal proteins reveal the structural features essential for stability under the extreme environments in which these organisms live, and will provide the structural basis required for stabilizing various mesophilic proteins for industrial applications. Here, we report the crystal structure of Pk-MGMT and structural comparison of Pk-MGMT and methyltransferase homologue from Escherichia coli (AdaC, C-terminal fragment of Ada protein). Analyses of solvent-accessible surface area (SASA) reveals a large discrepancy between Pk-MGMT and AdaC with respect to the property of the ASA. In the Pk-MGMT structure, the intra-helix ion-pairs contribute to reinforce stability of alpha-helices. The inter-helix ion-pairs exist in the interior of Pk-MGMT and stabilize internal packing of tertiary structure. Furthermore, structural features of helix cappings, intra and inter-helix ion-pairs are found around the active-site structure in Pk-MGMT.
Hyperthermostable protein structure maintained by intra and inter-helix ion-pairs in archaeal O6-methylguanine-DNA methyltransferase.,Hashimoto H, Inoue T, Nishioka M, Fujiwara S, Takagi M, Imanaka T, Kai Y J Mol Biol. 1999 Sep 24;292(3):707-16. PMID:10497033[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Leclere MM, Nishioka M, Yuasa T, Fujiwara S, Takagi M, Imanaka T. The O6-methylguanine-DNA methyltransferase from the hyperthermophilic archaeon Pyrococcus sp. KOD1: a thermostable repair enzyme. Mol Gen Genet. 1998 Apr;258(1-2):69-77. PMID:9613574
- ↑ Hashimoto H, Inoue T, Nishioka M, Fujiwara S, Takagi M, Imanaka T, Kai Y. Hyperthermostable protein structure maintained by intra and inter-helix ion-pairs in archaeal O6-methylguanine-DNA methyltransferase. J Mol Biol. 1999 Sep 24;292(3):707-16. PMID:10497033 doi:10.1006/jmbi.1999.3100
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