View source for 5z53


==Crystal structure of a cyclase Filc from Fischerella sp. in complex with cyclo-L-Arg-D-Pro==
<StructureSection load='5z53' size='340' side='right'caption='[[5z53]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5z53]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Fischerella_sp._TAU Fischerella sp. TAU]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z53 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]] 1.86&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0HZ:AMINO({3-[(3S,8AS)-1,4-DIOXOOCTAHYDROPYRROLO[1,2-A]PYRAZIN-3-YL]PROPYL}AMINO)METHANIMINIUM'>0HZ</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=5z53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z53 OCA], [https://pdbe.org/5z53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5z53 RCSB], [https://www.ebi.ac.uk/pdbsum/5z53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5z53 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1P8VSI6_9CYAN A0A1P8VSI6_9CYAN] 
<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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5z53" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fischerella sp. TAU]]
[[Category: Large Structures]]
[[Category: Chen CC]]
[[Category: Guo RT]]
[[Category: Hu XY]]
[[Category: Liu WD]]