3egi
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3egi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EGI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EGI FirstGlance]. <br> | <table><tr><td colspan='2'>[[3egi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EGI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EGI FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TGS1, HCA137, NCOA6IP, PIMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TGS1, HCA137, NCOA6IP, PIMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3egi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3egi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3egi RCSB], [http://www.ebi.ac.uk/pdbsum/3egi PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3egi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3egi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3egi RCSB], [http://www.ebi.ac.uk/pdbsum/3egi PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TGS1_HUMAN TGS1_HUMAN]] Catalyzes the 2 serial methylation steps for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Hypermethylation of the m7G cap of U snRNAs leads to their concentration in nuclear foci, their colocalization with coilin and the formation of canonical Cajal bodies (CBs). Plays a role in transcriptional regulation.<ref>PMID:11517327</ref> <ref>PMID:11912212</ref> <ref>PMID:16687569</ref> <ref>PMID:18775984</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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Structure analysis of the conserved methyltransferase domain of human trimethylguanosine synthase TGS1.,Monecke T, Dickmanns A, Strasser A, Ficner R Acta Crystallogr D Biol Crystallogr. 2009 Apr;65(Pt 4):332-8. Epub 2009 Mar 19. PMID:19307714<ref>PMID:19307714</ref> | Structure analysis of the conserved methyltransferase domain of human trimethylguanosine synthase TGS1.,Monecke T, Dickmanns A, Strasser A, Ficner R Acta Crystallogr D Biol Crystallogr. 2009 Apr;65(Pt 4):332-8. Epub 2009 Mar 19. PMID:19307714<ref>PMID:19307714</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Dickmanns, A | + | [[Category: Dickmanns, A]] |
| - | [[Category: Ficner, R | + | [[Category: Ficner, R]] |
| - | [[Category: Monecke, T | + | [[Category: Monecke, T]] |
[[Category: Alpha-beta-alpha sandwich]] | [[Category: Alpha-beta-alpha sandwich]] | ||
[[Category: Methyltransferase]] | [[Category: Methyltransferase]] | ||
Revision as of 07:59, 25 December 2014
Methyltransferase domain of human trimethylguanosine synthase TGS1 bound to m7GpppA (inactive form)
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