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| | <StructureSection load='1z3c' size='340' side='right'caption='[[1z3c]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1z3c' size='340' side='right'caption='[[1z3c]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1z3c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enccn Enccn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z3C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Z3C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1z3c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Encephalitozoon_cuniculi Encephalitozoon cuniculi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z3C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SA8:S-5-AZAMETHIONINE-5-DEOXYADENOSINE'>SA8</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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ri1|1ri1]], [[1ri2|1ri2]], [[1ri3|1ri3]], [[1ri4|1ri4]], [[1ri5|1ri5]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SA8:S-5-AZAMETHIONINE-5-DEOXYADENOSINE'>SA8</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECU10_0380 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6035 ENCCN])</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=1z3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z3c OCA], [https://pdbe.org/1z3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z3c RCSB], [https://www.ebi.ac.uk/pdbsum/1z3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z3c ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/mRNA_(guanine-N(7)-)-methyltransferase mRNA (guanine-N(7)-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.56 2.1.1.56] </span></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=1z3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z3c OCA], [http://pdbe.org/1z3c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z3c RCSB], [http://www.ebi.ac.uk/pdbsum/1z3c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z3c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MCES_ENCCU MCES_ENCCU]] mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.<ref>PMID:15760890</ref> | + | [https://www.uniprot.org/uniprot/MCES_ENCCU MCES_ENCCU] mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.<ref>PMID:15760890</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1z3c" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1z3c" style="background-color:#fffaf0;"></div> |
| - | | |
| - | ==See Also== | |
| - | *[[MRNA capping enzyme|MRNA capping enzyme]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Enccn]] | + | [[Category: Encephalitozoon cuniculi]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fabrega, C]] | + | [[Category: Fabrega C]] |
| - | [[Category: Hausmann, S]] | + | [[Category: Hausmann S]] |
| - | [[Category: Lima, C D]] | + | [[Category: Lima CD]] |
| - | [[Category: Schneller, S W]] | + | [[Category: Schneller SW]] |
| - | [[Category: Shuman, S]] | + | [[Category: Shuman S]] |
| - | [[Category: Zhang, S]] | + | [[Category: Zhang S]] |
| - | [[Category: Azoadomet]]
| + | |
| - | [[Category: Cap]]
| + | |
| - | [[Category: M7g]]
| + | |
| - | [[Category: Messenger rna cap]]
| + | |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Rna]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
MCES_ENCCU mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.[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 Encephalitozoon cuniculi mRNA cap (guanine N-7) methyltransferase Ecm1 has been characterized structurally but not biochemically. Here we show that purified Ecm1 is a monomeric protein that catalyzes methyl transfer from S-adenosylmethionine (AdoMet) to GTP. The reaction is cofactor-independent and optimal at pH 7.5. Ecm1 also methylates GpppA, GDP, and dGTP but not ATP, CTP, UTP, ITP, or m(7)GTP. The affinity of Ecm1 for the cap dinucleotide GpppA (K 0.1 mm) is higher than that for GTP (K(m) 1 mm) or GDP (K(m) 2.4 mm). Methylation of GTP by Ecm1 in the presence of 5 microm AdoMet is inhibited by the reaction product AdoHcy (IC(50) 4 microm) and by substrate analogs sinefungin (IC(50) 1.5 microm), aza-AdoMet (IC(50) 100 microm), and carbocyclic aza-AdoMet (IC(50) 35 microm). The crystal structure of an Ecm1.aza-AdoMet binary complex reveals that the inhibitor occupies the same site as AdoMet. Structure-function analysis of Ecm1 by alanine scanning and conservative substitutions identified functional groups necessary for methyltransferase activity in vivo. Amino acids Lys-54, Asp-70, Asp-78, and Asp-94, which comprise the AdoMet-binding site, and Phe-141, which contacts the cap guanosine, are essential for cap methyltransferase activity in vitro.
Encephalitozoon cuniculi mRNA cap (guanine N-7) methyltransferase: methyl acceptor specificity, inhibition BY S-adenosylmethionine analogs, and structure-guided mutational analysis.,Hausmann S, Zheng S, Fabrega C, Schneller SW, Lima CD, Shuman S J Biol Chem. 2005 May 27;280(21):20404-12. Epub 2005 Mar 9. PMID:15760890[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hausmann S, Zheng S, Fabrega C, Schneller SW, Lima CD, Shuman S. Encephalitozoon cuniculi mRNA cap (guanine N-7) methyltransferase: methyl acceptor specificity, inhibition BY S-adenosylmethionine analogs, and structure-guided mutational analysis. J Biol Chem. 2005 May 27;280(21):20404-12. Epub 2005 Mar 9. PMID:15760890 doi:10.1074/jbc.M501073200
- ↑ Hausmann S, Zheng S, Fabrega C, Schneller SW, Lima CD, Shuman S. Encephalitozoon cuniculi mRNA cap (guanine N-7) methyltransferase: methyl acceptor specificity, inhibition BY S-adenosylmethionine analogs, and structure-guided mutational analysis. J Biol Chem. 2005 May 27;280(21):20404-12. Epub 2005 Mar 9. PMID:15760890 doi:10.1074/jbc.M501073200
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