6dch
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of isonitrile biosynthesis enzyme ScoE== | |
| + | <StructureSection load='6dch' size='340' side='right' caption='[[6dch]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6dch]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DCH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DCH FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6dch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dch OCA], [http://pdbe.org/6dch PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dch RCSB], [http://www.ebi.ac.uk/pdbsum/6dch PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dch ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The electron-rich isonitrile is an important functionality in bioactive natural products, but its biosynthesis has been restricted to the IsnA family of isonitrile synthases. We here provide the first structural and biochemical evidence of an alternative mechanism for isonitrile formation. ScoE, a putative non-heme iron(II)-dependent enzyme from Streptomyces coeruleorubidus, was shown to catalyze the conversion of (R)-3-((carboxymethyl)amino)butanoic acid to (R)-3-isocyanobutanoic acid through an oxidative decarboxylation mechanism. This work further provides a revised scheme for the biosynthesis of a unique class of isonitrile lipopeptides, members of which are critical for the virulence of pathogenic mycobacteria. | ||
| - | + | Isonitrile Formation by a Non-heme Iron(II)-Dependent Oxidase/Decarboxylase.,Harris N, Born D, Cai W, Huang Y, Martin J, Khalaf R, Drennan C, Zhang W Angew Chem Int Ed Engl. 2018 Jun 15. doi: 10.1002/anie.201804307. PMID:29906336<ref>PMID:29906336</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6dch" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Born, D A]] | ||
| + | [[Category: Drennan, C L]] | ||
| + | [[Category: Enzyme]] | ||
| + | [[Category: Isonitrile]] | ||
| + | [[Category: Metalloenzyme]] | ||
| + | [[Category: Non-heme iron]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 05:37, 27 June 2018
Structure of isonitrile biosynthesis enzyme ScoE
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