5yvl: Difference between revisions

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-'''Unreleased structure'''
-The entry 5yvl is ON HOLD  until Nov 26 2019
+==Crystal structure of Enzyme A in complex with ligand PEG==
+<StructureSection load='5yvl' size='340' side='right' caption='[[5yvl]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5yvl]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YVL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YVL FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</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=5yvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yvl OCA], [http://pdbe.org/5yvl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yvl RCSB], [http://www.ebi.ac.uk/pdbsum/5yvl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yvl ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Found recently in stignomatales, the Stig cyclases catalyze the Cope rearrangement and intramolecular cyclization to produce complex indole alkaloids. Five crystal structures were solved of subfamily 1 and 2 Stig cyclases, which adopt a beta-sandwich fold like the non-catalytic carbohydrate-binding motif. Several complex structures were also determined of indole-based compounds, which are bound to the hydrophobic terminal cavity, where a conserved Asp residue makes an H-bond to the indole N and triggers the acid-catalyzed Cope rearrangement. Through analyzing the enzyme-ligand interactions and mutagenesis experiments, several aromatic residues were found important in catalysis. Apart from a common substrate binding mode and catalytic mechanism, potential subfamily variations that may attribute to the different product specificity are implicated. These results shall expand our scope of enzymology, in particular for further investigation of the biosynthetic Cope rearrangement.
-Authors: Hu, X.Y., Liu, W.D., Chen, C.C., Guo, R.T.
+The Crystal Structure of a Class of Cyclases that Catalyze the Cope Rearrangement.,Chen CC, Hu X, Tang X, Yang Y, Ko TP, Gao J, Zheng Y, Huang JW, Yu Z, Li L, Han S, Cai N, Zhang Y, Liu W, Guo RT Angew Chem Int Ed Engl. 2018 Nov 12;57(46):15060-15064. doi:, 10.1002/anie.201808231. Epub 2018 Oct 23. PMID:30222239<ref>PMID:30222239</ref>
-Description: Crystal structure of Enzyme A in complex with ligand PEG
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Chen, C.C]]
+<div class="pdbe-citations 5yvl" style="background-color:#fffaf0;"></div>
-[[Category: Hu, X.Y]]
+== References ==
-[[Category: Guo, R.T]]
+<references/>
-[[Category: Liu, W.D]]
+__TOC__
+</StructureSection>
+[[Category: Chen, C C]]
+[[Category: Guo, R T]]
+[[Category: Hu, X Y]]
+[[Category: Liu, W D]]
+[[Category: Prenyltransferase]]
+[[Category: Transferase]]