3x0d
From Proteopedia
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| - | ''' | + | ==Crystal structure of C.elegans PRMT7 in complex with SAH (P43212)== |
| + | <StructureSection load='3x0d' size='340' side='right' caption='[[3x0d]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3x0d]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3wss 3wss]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3X0D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3X0D FirstGlance]. <br> | ||
| + | </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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3x0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x0d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3x0d RCSB], [http://www.ebi.ac.uk/pdbsum/3x0d 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: Hasegawa, M.]] | ||
| + | [[Category: Shimizu, T.]] | ||
| + | [[Category: Toma-Fukai, S.]] | ||
| + | [[Category: Rossmann fold]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 11:09, 29 October 2014
Crystal structure of C.elegans PRMT7 in complex with SAH (P43212)
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