6a9f

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'''Unreleased structure'''
 
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The entry 6a9f is ON HOLD until Paper Publication
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==Crystal of a protein structure from Fischerella in complex with ligand4==
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<StructureSection load='6a9f' size='340' side='right' caption='[[6a9f]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6a9f]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A9F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A9F FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9BF:4-(1~{H}-indol-3-yl)butan-2-one'>9BF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<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=6a9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a9f OCA], [http://pdbe.org/6a9f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a9f RCSB], [http://www.ebi.ac.uk/pdbsum/6a9f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a9f ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Hu, X.Y., Liu, W.D., Chen, C.C., Guo, R.T.
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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>
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Description: Crystal of a protein structure from Fischerella in complex with ligand4
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Hu, X.Y]]
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<div class="pdbe-citations 6a9f" style="background-color:#fffaf0;"></div>
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[[Category: Liu, W.D]]
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== References ==
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[[Category: Chen, C.C]]
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<references/>
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[[Category: Guo, R.T]]
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__TOC__
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</StructureSection>
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[[Category: Chen, C C]]
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[[Category: Guo, R T]]
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[[Category: Hu, X Y]]
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[[Category: Liu, W D]]
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[[Category: Prenyltransferase]]
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[[Category: Transferase]]

Revision as of 08:16, 19 December 2018

Crystal of a protein structure from Fischerella in complex with ligand4

6a9f, resolution 1.70Å

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