9v4i: Difference between revisions
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==Prenyltransferase Ord1 D219A== | |||
<StructureSection load='9v4i' size='340' side='right'caption='[[9v4i]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9v4i]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Unclassified_Streptomyces Unclassified Streptomyces]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9V4I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9V4I FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9v4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9v4i OCA], [https://pdbe.org/9v4i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9v4i RCSB], [https://www.ebi.ac.uk/pdbsum/9v4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9v4i ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Enzymes are involved in the biosynthesis of a variety of secondary metabolites found in nature. The catalytic mechanism is regulated by the three-dimensional structure of the enzyme, particularly at the catalytic site, resulting in the synthesis of natural products with complex conformations derived from a regioselective, chemoselective, or stereoselective preference of the enzyme reaction. Prenyltransferase, which belongs to the prenylsynthase superfamily, catalyzes the condensation of isoprene to an aromatic compound, consequently producing a terpenoid scaffold structure. Prenyltransferase thus plays an important role in expanding the chemical diversity of the terpenoids. Although the three-dimensional structures of prenylsynthases categorized in the same superfamily have been resolved, the catalytic mechanism of prenyltransferase has been veiled. In this study, we determined the X-ray crystal structure of a novel prenyltransferase, Ord1, which is derived from Streptomyces. Here, we report the enzymatic characteristics of the Ord1 and discuss its catalytic mechanism. | |||
Structure-Activity Relationship of an All-alpha-helical Prenyltransferase Reveals the Mechanism of Indole Prenylation.,Oshiro T, Uehara S, Suto A, Tanaka Y, Ito T, Kodera Y, Matsui T Biochemistry. 2025 Sep 18. doi: 10.1021/acs.biochem.5c00329. PMID:40968638<ref>PMID:40968638</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9v4i" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Unclassified Streptomyces]] | |||
[[Category: Ito T]] | |||
[[Category: Kodera Y]] | |||
[[Category: Matsui T]] | |||
[[Category: Oshiro T]] | |||
[[Category: Tanaka Y]] | |||
[[Category: Uehara S]] | |||
