6zrx: Difference between revisions
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<StructureSection load='6zrx' size='340' side='right'caption='[[6zrx]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='6zrx' size='340' side='right'caption='[[6zrx]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6zrx]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6zrx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonospora_olivasterospora Micromonospora olivasterospora]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZRX FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6C7:S-(3-METHYLBUT-2-EN-1-YL)+TRIHYDROGEN+THIODIPHOSPHATE'>6C7</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6C7:S-(3-METHYLBUT-2-EN-1-YL)+TRIHYDROGEN+THIODIPHOSPHATE'>6C7</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6zrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zrx OCA], [https://pdbe.org/6zrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zrx RCSB], [https://www.ebi.ac.uk/pdbsum/6zrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zrx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q2MFY2_MICOL Q2MFY2_MICOL] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6zrx" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6zrx" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Micromonospora olivasterospora]] | ||
[[Category: | [[Category: Ostertag E]] | ||
[[Category: | [[Category: Stehle T]] | ||
[[Category: | [[Category: Zocher G]] | ||
Latest revision as of 14:57, 1 February 2024
Crystal structure of 6-dimethylallyltryptophan synthase from Micromonospora olivasterospora in complex with DMASPP and TrpCrystal structure of 6-dimethylallyltryptophan synthase from Micromonospora olivasterospora in complex with DMASPP and Trp
Structural highlights
FunctionPublication Abstract from PubMedPrenylation 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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