6a92: Difference between revisions
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==Crystal structure of a cyclase Filc1 from Fischerella sp.== | |||
<StructureSection load='6a92' size='340' side='right'caption='[[6a92]], [[Resolution|resolution]] 1.58Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6a92]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Fischerella Fischerella]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A92 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]] 1.58Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=6a92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a92 OCA], [https://pdbe.org/6a92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a92 RCSB], [https://www.ebi.ac.uk/pdbsum/6a92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a92 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6a92" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Fischerella]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen CC]] | |||
[[Category: Guo RT]] | |||
[[Category: Hu XY]] | |||
[[Category: Liu WD]] | |||
Latest revision as of 12:21, 22 November 2023
Crystal structure of a cyclase Filc1 from Fischerella sp.Crystal structure of a cyclase Filc1 from Fischerella sp.
Structural highlights
FunctionPublication Abstract from PubMedFound 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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