3x0d

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==Crystal structure of C.elegans PRMT7 in complex with SAH (P43212)==
==Crystal structure of C.elegans PRMT7 in complex with SAH (P43212)==
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<StructureSection load='3x0d' size='340' side='right' caption='[[3x0d]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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<StructureSection load='3x0d' size='340' side='right'caption='[[3x0d]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3x0d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. 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>
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<table><tr><td colspan='2'>[[3x0d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3X0D FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
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<tr id='gene'><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 id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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://pdbe.org/3x0d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3x0d RCSB], [http://www.ebi.ac.uk/pdbsum/3x0d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3x0d ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3x0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x0d OCA], [https://pdbe.org/3x0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3x0d RCSB], [https://www.ebi.ac.uk/pdbsum/3x0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3x0d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ANM7_CAEEL ANM7_CAEEL]] Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA) (By similarity).
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[https://www.uniprot.org/uniprot/ANM7_CAEEL ANM7_CAEEL] Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA) (By similarity).
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3x0d" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Caeel]]
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[[Category: Caenorhabditis elegans]]
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[[Category: Hasegawa, M]]
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[[Category: Large Structures]]
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[[Category: Shimizu, T]]
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[[Category: Hasegawa M]]
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[[Category: Toma-Fukai, S]]
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[[Category: Shimizu T]]
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[[Category: Rossmann fold]]
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[[Category: Toma-Fukai S]]
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[[Category: Transferase]]
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Current revision

Crystal structure of C.elegans PRMT7 in complex with SAH (P43212)

PDB ID 3x0d

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