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3r0q

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==A Uniquely Open Conformation Revealed in the Crystal Structure of Arabidopsis Thaliana Protein Arginine Methyltransferase 10==
==A Uniquely Open Conformation Revealed in the Crystal Structure of Arabidopsis Thaliana Protein Arginine Methyltransferase 10==
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<StructureSection load='3r0q' size='340' side='right' caption='[[3r0q]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
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<StructureSection load='3r0q' size='340' side='right'caption='[[3r0q]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3r0q]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R0Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R0Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3r0q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R0Q 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></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]] 2.61&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRMT4.2, At1g04870, F13M7.14, F13M7_12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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></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=3r0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r0q OCA], [http://pdbe.org/3r0q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3r0q RCSB], [http://www.ebi.ac.uk/pdbsum/3r0q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3r0q 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=3r0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r0q OCA], [https://pdbe.org/3r0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r0q RCSB], [https://www.ebi.ac.uk/pdbsum/3r0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r0q ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ANM10_ARATH ANM10_ARATH]] Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins. Essential for regulating flowering time.<ref>PMID:21986201</ref>
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[https://www.uniprot.org/uniprot/ANM10_ARATH ANM10_ARATH] Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins. Essential for regulating flowering time.<ref>PMID:21986201</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Protein arginine methyltransferase 10 (PRMT10) is a type I arginine methyltransferase that is essential for regulating flowering time in Arabidopsis thaliana. We present a 2.6 A resolution crystal structure of A. thaliana PRMT 10 (AtPRMT10) in complex with a reaction product, S-adenosylhomocysteine. The structure reveals a dimerization arm that is 12-20 residues longer than PRMT structures elucidated previously; as a result, the essential AtPRMT10 dimer exhibits a large central cavity and a distinctly accessible active site. We employ molecular dynamics to examine how dimerization facilitates AtPRMT10 motions necessary for activity, and we show that these motions are conserved in other PRMT enzymes. Finally, functional data reveal that the 10 N-terminal residues of AtPRMT10 influence substrate specificity, and that enzyme activity is dependent on substrate protein sequences distal from the methylation site. Taken together, these data provide insights into the molecular mechanism of AtPRMT10, as well as other members of the PRMT family of enzymes. They highlight differences between AtPRMT10 and other PRMTs but also indicate that motions are a conserved element of PRMT function.
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Crystal Structure of the Plant Epigenetic Protein Arginine Methyltransferase 10.,Cheng Y, Frazier M, Lu F, Cao X, Redinbo MR J Mol Biol. 2011 Oct 1. PMID:21986201<ref>PMID:21986201</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 3r0q" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arath]]
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[[Category: Arabidopsis thaliana]]
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[[Category: Cheng, Y]]
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[[Category: Large Structures]]
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[[Category: Redinbo, M R]]
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[[Category: Cheng Y]]
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[[Category: Arginine methyltransferase]]
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[[Category: Redinbo MR]]
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[[Category: Methylation]]
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[[Category: Transferase]]
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Current revision

A Uniquely Open Conformation Revealed in the Crystal Structure of Arabidopsis Thaliana Protein Arginine Methyltransferase 10

PDB ID 3r0q

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