5ynu: Difference between revisions

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-'''Unreleased structure'''
-The entry 5ynu is ON HOLD  until Oct 25 2019
+==Crystal structure of an aromatic prenyltransferase in complex with ligand1==
+<StructureSection load='5ynu' size='340' side='right' caption='[[5ynu]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5ynu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YNU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YNU 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=DMA:DIMETHYLALLYL+DIPHOSPHATE'>DMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></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=5ynu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ynu OCA], [http://pdbe.org/5ynu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ynu RCSB], [http://www.ebi.ac.uk/pdbsum/5ynu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ynu 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.
-Authors: Wang, J., Liu, W.D., Chen, C.C., Guo, R.T.
+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>
-Description: Crystal structure of an aromatic prenyltransferase in complex with ligand1
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Liu, W.D]]
+<div class="pdbe-citations 5ynu" style="background-color:#fffaf0;"></div>
-[[Category: Chen, C.C]]
+== References ==
-[[Category: Guo, R.T]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Chen, C C]]
+[[Category: Guo, R T]]
+[[Category: Liu, W D]]
 [[Category: Wang, J]]
+[[Category: Prenyltransferase]]
+[[Category: Transferase]]