3wst
From Proteopedia
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| - | + | ==Crystal structure of C.elegans PRMT7 in complex with SAH(P31)== | |
| - | + | <StructureSection load='3wst' size='340' side='right' caption='[[3wst]], [[Resolution|resolution]] 2.39Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3wst]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WST OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WST FirstGlance]. <br> | |
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pmrt-2, prmt-7, W06D4.4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=3wst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wst OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wst RCSB], [http://www.ebi.ac.uk/pdbsum/3wst PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Protein arginine methyltransferase 7 (PRMT7) is a member of a family of enzymes that catalyze the transfer of methyl groups from S-adenosyl-l-methionine to nitrogen atoms on arginine residues. Here, we describe the crystal structure of Caenorhabditis elegans PRMT7 in complex with its reaction product S-adenosyl-l-homocysteine. The structural data indicated that PRMT7 harbors two tandem repeated PRMT core domains that form a novel homodimer-like structure. S-adenosyl-l-homocysteine bound to the N-terminal catalytic site only; the C-terminal catalytic site is occupied by a loop that inhibits cofactor binding. Mutagenesis demonstrated that only the N-terminal catalytic site of PRMT7 is responsible for cofactor binding. | ||
| - | + | Protein arginine methyltransferase 7 has a novel homodimer-like structure formed by tandem repeats.,Hasegawa M, Toma-Fukai S, Kim JD, Fukamizu A, Shimizu T FEBS Lett. 2014 Apr 9. pii: S0014-5793(14)00272-5. doi:, 10.1016/j.febslet.2014.03.053. PMID:24726727<ref>PMID:24726727</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Caeel]] | ||
[[Category: Hasegawa, M.]] | [[Category: Hasegawa, M.]] | ||
[[Category: Shimizu, T.]] | [[Category: Shimizu, T.]] | ||
Revision as of 05:17, 18 June 2014
Crystal structure of C.elegans PRMT7 in complex with SAH(P31)
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