4pip: Difference between revisions

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'''Unreleased structure'''
==Engineered EgtD variant EgtD-M252V,E282A in complex with tryptophan and SAH==
<StructureSection load='4pip' size='340' side='right' caption='[[4pip]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4pip]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PIP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PIP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pim|4pim]], [[4pin|4pin]], [[4pio|4pio]]</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=4pip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pip OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pip RCSB], [http://www.ebi.ac.uk/pdbsum/4pip 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 4pip 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: HyoA (engineered EgtD double mutant M252V, E282A) in complex with tryptophan and SAH
== 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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