4pin: Difference between revisions

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'''Unreleased structure'''
==Ergothioneine-biosynthetic methyltransferase EgtD in complex with N,N-dimethylhistidine==
<StructureSection load='4pin' size='340' side='right' caption='[[4pin]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4pin]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PIN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PIN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AVI:N,N-DIMETHYL-L-HISTIDINE'>AVI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pim|4pim]], [[4pio|4pio]], [[4pip|4pip]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-histidine_N(alpha)-methyltransferase L-histidine N(alpha)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.44 2.1.1.44] </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=4pin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pin OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pin RCSB], [http://www.ebi.ac.uk/pdbsum/4pin PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ergothioneine is an N-alpha-trimethyl-2-thiohistidine derivative that occurs in human, plant, fungal, and bacterial cells. Biosynthesis of this redox-active betaine starts with trimethylation of the alpha-amino group of histidine. The three consecutive methyl transfers are catalyzed by the S-adenosylmethionine-dependent methyltransferase EgtD. Three crystal structures of this enzyme in the absence and in the presence of N-alpha-dimethylhistidine and S-adenosylhomocysteine implicate a preorganized array of hydrophilic interactions as the determinants for substrate specificity and apparent processivity. We identified two active site mutations that change the substrate specificity of EgtD 107 -fold and transform the histidine-methyltransferase into a proficient tryptophan-methyltransferase. Finally, a genomic search for EgtD homologues in fungal genomes revealed tyrosine and tryptophan trimethylation activity as a frequent trait in ascomycetous and basidomycetous fungi.


The entry 4pin is ON HOLD  until Paper Publication
Ergothioneine Biosynthetic Methyltransferase EgtD Reveals the Structural Basis of Aromatic Amino Acid Betaine Biosynthesis.,Vit A, Misson L, Blankenfeldt W, Seebeck FP Chembiochem. 2014 Nov 17. doi: 10.1002/cbic.201402522. PMID:25404173<ref>PMID:25404173</ref>


Authors: Vit, A., Seebeck, F.P., Blankenfeldt, W.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Ergothioneine-biosynthetic methyltransferase EgtD in complex with N,N-dimethylhistidine
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Blankenfeldt, W]]
[[Category: Seebeck, F P]]
[[Category: Vit, A]]
[[Category: Ergothioneine]]
[[Category: Histidine betaine]]
[[Category: Methyltransferase]]
[[Category: Transferase]]
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