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| | <StructureSection load='3gcz' size='340' side='right'caption='[[3gcz]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='3gcz' size='340' side='right'caption='[[3gcz]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3gcz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Yokase_virus Yokase virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GCZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3GCZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3gcz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yokose_virus Yokose virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GCZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <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]] 1.7Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/mRNA_(nucleoside-2'-O)-methyltransferase mRNA (nucleoside-2'-O)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.57 2.1.1.57] </span></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <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'>[http://proteopedia.org/fgij/fg.htm?mol=3gcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gcz OCA], [http://pdbe.org/3gcz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gcz RCSB], [http://www.ebi.ac.uk/pdbsum/3gcz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gcz 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=3gcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gcz OCA], [https://pdbe.org/3gcz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gcz RCSB], [https://www.ebi.ac.uk/pdbsum/3gcz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gcz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q7T918_9FLAV Q7T918_9FLAV] |
| | == 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: Yokase virus]] | + | [[Category: Yokose virus]] |
| - | [[Category: Bollati, M]] | + | [[Category: Bollati M]] |
| - | [[Category: Bolognesi, M]] | + | [[Category: Bolognesi M]] |
| - | [[Category: Mastrangelo, E]] | + | [[Category: Mastrangelo E]] |
| - | [[Category: Milani, M]] | + | [[Category: Milani M]] |
| - | [[Category: SPINE, Structural Proteomics in Europe]]
| + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Flavivirus]]
| + | |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Rna capping]]
| + | |
| - | [[Category: Rna replication]]
| + | |
| - | [[Category: Spine]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Structural proteomics in europe]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Viral enzyme structure]]
| + | |
| Structural highlights
Function
Q7T918_9FLAV
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
Presently known flaviviruses belong to three major evolutionary branches: tick-borne viruses, mosquito-borne viruses and viruses with no known vector. Here we present the crystal structure of the Yokose virus methyltransferase at 1.7A resolution, the first structure of a methyltransferase of a Flavivirus with no known vector. Structural comparison of three methyltransferases representative of each of the Flavivirus branches shows that fold and structures are closely conserved, most differences being related to surface loops flexibility. Analysis of the conserved residues throughout all the sequenced flaviviral methyltransferases reveals that, besides the central cleft hosting the substrate and cofactor binding sites, a second, almost continuous, patch is conserved and points away from active site towards the back of the protein. The high level of structural conservation in this region could be functional for the methyltransferase/RNA interaction and stabilization of the ensuing complex.
Crystal structure of a methyltransferase from a no-known-vector Flavivirus.,Bollati M, Milani M, Mastrangelo E, de Lamballerie X, Canard B, Bolognesi M Biochem Biophys Res Commun. 2009 Apr 24;382(1):200-4. Epub 2009 Mar 9. PMID:19275894[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bollati M, Milani M, Mastrangelo E, de Lamballerie X, Canard B, Bolognesi M. Crystal structure of a methyltransferase from a no-known-vector Flavivirus. Biochem Biophys Res Commun. 2009 Apr 24;382(1):200-4. Epub 2009 Mar 9. PMID:19275894 doi:10.1016/j.bbrc.2009.03.008
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