5yvk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5yvk is ON HOLD until Nov 26 2019
+
==Crystal structure of Enzyme A in complex with ligand2==
 +
<StructureSection load='5yvk' size='340' side='right' caption='[[5yvk]], [[Resolution|resolution]] 1.29&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[5yvk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YVK FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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></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=5yvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yvk OCA], [http://pdbe.org/5yvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yvk RCSB], [http://www.ebi.ac.uk/pdbsum/5yvk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yvk 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 ligand2
+
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 5yvk" 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]]

Revision as of 12:08, 7 November 2018

Crystal structure of Enzyme A in complex with ligand2

5yvk, resolution 1.29Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5yvk"
Personal tools