6a98: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of an apo form Enzyme from Fischerella== | |||
<StructureSection load='6a98' size='340' side='right' caption='[[6a98]], [[Resolution|resolution]] 1.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6a98]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A98 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6a98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a98 OCA], [http://pdbe.org/6a98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a98 RCSB], [http://www.ebi.ac.uk/pdbsum/6a98 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a98 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. | |||
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: Hu, X | <div class="pdbe-citations 6a98" style="background-color:#fffaf0;"></div> | ||
[[Category: Liu, W | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Chen, C C]] | |||
[[Category: Guo, R T]] | |||
[[Category: Hu, X Y]] | |||
[[Category: Liu, W D]] | |||
[[Category: Prenyltransferase]] | |||
[[Category: Transferase]] | |||
Revision as of 11:15, 19 December 2018
Crystal structure of an apo form Enzyme from FischerellaCrystal structure of an apo form Enzyme from Fischerella
Structural highlights
Publication 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
|
| ||||||||||||||||