1f3l: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1f3l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F3L FirstGlance]. <br> | <table><tr><td colspan='2'>[[1f3l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F3L FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>< | </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> | ||
<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=1f3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f3l RCSB], [http://www.ebi.ac.uk/pdbsum/1f3l PDBsum]</span></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=1f3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f3l RCSB], [http://www.ebi.ac.uk/pdbsum/1f3l PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Cheng, X | [[Category: Cheng, X]] | ||
[[Category: Zhang, X | [[Category: Zhang, X]] | ||
[[Category: Zhou, L | [[Category: Zhou, L]] | ||
[[Category: Arginine methyltransferase]] | [[Category: Arginine methyltransferase]] | ||
[[Category: Beta barrel]] | [[Category: Beta barrel]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 23:39, 22 December 2014
CRYSTAL STRUCTURE OF THE CONSERVED CORE OF PROTEIN ARGININE METHYLTRANSFERASE PRMT3CRYSTAL STRUCTURE OF THE CONSERVED CORE OF PROTEIN ARGININE METHYLTRANSFERASE PRMT3
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProtein arginine methylation has been implicated in signal transduction, nuclear transport and transcription regulation. Protein arginine methyltransferases (PRMTs) mediate the AdoMet-dependent methylation of many proteins, including many RNA binding proteins involved in various aspects of RNA processing and/or transport. Here we describe the crystal structure of the rat PRMT3 catalytic core in complex with reaction product AdoHcy, determined at 2.0 A resolution. The results reveal a two-domain structure: an AdoMet-binding domain and a barrel-like domain. The AdoMet-binding domain is a compact version of the consensus AdoMet-dependent methyltransferase fold. The active site is situated in a cone-shaped pocket between the two domains. The residues that make up the active site are conserved across the PRMT family, consisting of a double-E loop containing two invariant Glu and one His-Asp proton-relay system. The structure suggests a mechanism for the methylation reaction and provides the structural basis for functional characterization of the PRMT family. In addition, crystal packing and solution behavior suggest dimer formation of the PRMT3 core. Crystal structure of the conserved core of protein arginine methyltransferase PRMT3.,Zhang X, Zhou L, Cheng X EMBO J. 2000 Jul 17;19(14):3509-19. PMID:10899106[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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