6zry
From Proteopedia
(Difference between revisions)
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==6-dimethylallyl tryptophan synthase== | ==6-dimethylallyl tryptophan synthase== | ||
- | <StructureSection load='6zry' size='340' side='right'caption='[[6zry]]' scene=''> | + | <StructureSection load='6zry' size='340' side='right'caption='[[6zry]], [[Resolution|resolution]] 1.65Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZRY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZRY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6zry]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_21819 Atcc 21819]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZRY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZRY FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6zry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zry OCA], [http://pdbe.org/6zry PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zry RCSB], [http://www.ebi.ac.uk/pdbsum/6zry PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zry ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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"><div style='overflow: auto; max-height: 3em;'>[[6zrx|6zrx]]</div></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MolI14.36, JD77_02062 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1880 ATCC 21819])</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6zry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zry OCA], [http://pdbe.org/6zry PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zry RCSB], [http://www.ebi.ac.uk/pdbsum/6zry PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zry ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Prenylation is a process widely prevalent in primary and secondary metabolism, contributing to functionality and chemical diversity in natural systems. Due to their high regio- and chemoselectivities, prenyltransferases are also valuable tools for creation of new compounds by chemoenzymatic synthesis and synthetic biology. Over the last ten years, biochemical and structural investigations shed light on the mechanism and key residues that control the catalytic process, but to date crucial information on how certain prenyltransferases control regioselectivity and chemoselectivity was still lacking. Here, we advance a general understanding of the enzyme family by contributing the first structure of a tryptophan C5-prenyltransferase 5-DMATS. Additinallyi, the structure of a bacterial tryptophan C6-prenyltransferase 6-DMATS was solved. Analysis and comparison of both substrate-bound complexes led to the identification of key residues for catalysis. Next, site-directed mutagenesis was successfully implemented to not only modify the prenyl donor specificity but also to redirect the prenylation, thereby switching the regioselectivity of 6-DMATS to that of 5-DMATS. The general strategy of structure-guided protein engineering should be applicable to other related prenyltransferases, thus enabling the production of novel prenylated compounds. | ||
+ | |||
+ | Reprogramming substrate and catalytic promiscuity of tryptophan prenyltransferases.,Ostertag E, Zheng L, Broger K, Stehle T, Li SM, Zocher G J Mol Biol. 2020 Nov 26. pii: S0022-2836(20)30644-6. doi:, 10.1016/j.jmb.2020.11.025. PMID:33249189<ref>PMID:33249189</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6zry" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Atcc 21819]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Ostertag E]] | + | [[Category: Ostertag, E]] |
- | [[Category: Stehle T]] | + | [[Category: Stehle, T]] |
- | [[Category: Zocher G]] | + | [[Category: Zocher, G]] |
+ | [[Category: Abba-barrel fold]] | ||
+ | [[Category: Complex]] | ||
+ | [[Category: Prenyltransferase]] | ||
+ | [[Category: Transferase]] |
Revision as of 07:01, 30 December 2020
6-dimethylallyl tryptophan synthase
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