9v4g
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Prenyltransferase Ord1 wild type== | |
| + | <StructureSection load='9v4g' size='340' side='right'caption='[[9v4g]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9v4g]] 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=9V4G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9V4G 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]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=9v4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9v4g OCA], [https://pdbe.org/9v4g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9v4g RCSB], [https://www.ebi.ac.uk/pdbsum/9v4g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9v4g 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 9v4g" 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]] | ||
Current revision
Prenyltransferase Ord1 wild type
| |||||||||||
