5ynw
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of an aromatic prenyltransferase in complex with ligand1 and 2== | |
| + | <StructureSection load='5ynw' size='340' side='right' caption='[[5ynw]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ynw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YNW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YNW FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8XL:3-[(Z)-2-isocyanoethenyl]-1H-indole'>8XL</scene>, <scene name='pdbligand=DST:DIMETHYLALLYL+S-THIOLODIPHOSPHATE'>DST</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ynt|5ynt]], [[5ynv|5ynv]], [[5ynu|5ynu]]</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=5ynw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ynw OCA], [http://pdbe.org/5ynw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ynw RCSB], [http://www.ebi.ac.uk/pdbsum/5ynw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ynw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | FamD1 is a novel CloQ/NphB-family indole prenyltransferase which involves in hapalindole-type alkaloid biosynthesis. Here the native FamD1 structure and three protein-ligand complexes are analyzed to investigate the molecular basis of substrate binding and catalysis. FamD1 adopts a typical ABBA architecture of aromatic prenyltransferase, in which the substrate-binding chamber is found in the central beta-barrel. The indole-containing acceptor substrate is bound adjacent to the prenyl donor. Based on the complex structures, a catalytic mechanism of FamD1 is proposed. Functional implications on the sister enzyme FamD2 are also discussed. | ||
| - | + | Structural insight into a novel indole prenyltransferase in hapalindole-type alkaloid biosynthesis.,Wang J, Chen CC, Yang Y, Liu W, Ko TP, Shang N, Hu X, Xie Y, Huang JW, Zhang Y, Guo RT Biochem Biophys Res Commun. 2018 Jan 8;495(2):1782-1788. doi:, 10.1016/j.bbrc.2017.12.039. Epub 2017 Dec 8. PMID:29229390<ref>PMID:29229390</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5ynw" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chen, C C]] | ||
| + | [[Category: Guo, R T]] | ||
| + | [[Category: Liu, W D]] | ||
[[Category: Wang, J]] | [[Category: Wang, J]] | ||
| + | [[Category: Prenyltransferase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 07:18, 29 August 2018
Crystal structure of an aromatic prenyltransferase in complex with ligand1 and 2
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