1eam: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1eam]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EAM FirstGlance]. <br> | <table><tr><td colspan='2'>[[1eam]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EAM FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase Polynucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.19 2.7.7.19] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase Polynucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.19 2.7.7.19] </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=1eam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eam OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eam RCSB], [http://www.ebi.ac.uk/pdbsum/1eam 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=1eam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eam OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eam RCSB], [http://www.ebi.ac.uk/pdbsum/1eam PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Polynucleotide adenylyltransferase]] | [[Category: Polynucleotide adenylyltransferase]] | ||
[[Category: Vaccinia virus]] | [[Category: Vaccinia virus]] | ||
[[Category: Gershon, P D | [[Category: Gershon, P D]] | ||
[[Category: Hodel, A E | [[Category: Hodel, A E]] | ||
[[Category: Hu, G | [[Category: Hu, G]] | ||
[[Category: Quiocho, F A | [[Category: Quiocho, F A]] | ||
[[Category: Methylated guanosine]] | [[Category: Methylated guanosine]] | ||
[[Category: Methyltransferase mutant e233a]] | [[Category: Methyltransferase mutant e233a]] | ||
Revision as of 03:21, 23 December 2014
VACCINIA METHYLTRANSFERASE VP39 MUTANT (EC: 2.7.7.19)VACCINIA METHYLTRANSFERASE VP39 MUTANT (EC: 2.7.7.19)
Structural highlights
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 PubMedWe have determined, by high resolution x-ray analysis, 10 structures comprising the mRNA cap-specific methyltransferase VP39 or specific mutants thereof in the presence of methylated nucleobase analogs (N1-methyladenine, N3-methyladenine, N1-methylcytosine, N3-methylcytosine) and their unmethylated counterparts, or nucleoside N7-methylguanosine. Together with solution affinity studies and previous crystallographic data for N7-methylguanosine and its phosphorylated derivatives, these data demonstrate that only methylated, positively charged bases are bound, indicating that their enhanced stacking with two aromatic side chains of VP39 (Tyr 22 and Phe 180) plays a dominant role in cap recognition. Four key features characterize this stacking interaction: (i) near perfect parallel alignment between the sandwiched methylated bases and aromatic side chains, (ii) substantial areas of overlap in the two-stacked rings, (iii) a 3.4-A interplanar spacing within the overlapping region, and (iv) positive charge in the heterocyclic nucleobase. mRNA cap recognition: dominant role of enhanced stacking interactions between methylated bases and protein aromatic side chains.,Hu G, Gershon PD, Hodel AE, Quiocho FA Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7149-54. PMID:10377383[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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