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| - | ==Crystal structure of C.elegans PRMT7 in complex with SAH (P43212)==
| + | #REDIRECT [[3x0d]] This PDB entry is obsolete and replaced by 3x0d |
| - | <StructureSection load='3wss' size='340' side='right' caption='[[3wss]], [[Resolution|resolution]] 2.15Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[3wss]] is a 1 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=3WSS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WSS FirstGlance]. <br>
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| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene><br>
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| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wst|3wst]]</td></tr>
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| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">prmt-7, pmrt-2, W06D4.4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr>
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| - | <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=3wss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wss OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wss RCSB], [http://www.ebi.ac.uk/pdbsum/3wss PDBsum]</span></td></tr>
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| - | <table>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | 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.
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| - | 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>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Caeel]]
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| - | [[Category: Hasegawa, M.]]
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| - | [[Category: Shimizu, T.]]
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| - | [[Category: Toma-fukai, S.]]
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| - | [[Category: Rossmann fold]]
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| - | [[Category: Transferase]]
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