This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3x0d
From Proteopedia
(Difference between revisions)
m (Protected "3x0d" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | ''' | + | ==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)
| |||||||||||
