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6rz2
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==SalL with Chloroadenosine== | |
| + | <StructureSection load='6rz2' size='340' side='right'caption='[[6rz2]], [[Resolution|resolution]] 1.77Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6rz2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Salinispora_tropica_CNB-440 Salinispora tropica CNB-440]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RZ2 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]] 1.77Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5CD:5-CHLORO-5-DEOXYADENOSINE'>5CD</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=6rz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rz2 OCA], [https://pdbe.org/6rz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rz2 RCSB], [https://www.ebi.ac.uk/pdbsum/6rz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rz2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SALL_SALTO SALL_SALTO] Involved in the biosynthesis of the proteosome inhibitor salinosporamide A (SalA). Catalyzes the halogenation of S-adenosyl-L-methionine (SAM) with chloride to generate 5'-chloro-5'-deoxyadenosine (5'-CIDA) and L-methionine. It can also use bromide and iodide, producing halogenated 5'-deoxyadenosine (5'-XDA) and L-methionine, however no halogenase activity is detected in the presence of fluoride.<ref>PMID:18059261</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A tandem enzymatic strategy to enhance the scope of C-alkylation of small molecules via the in situ formation of S-adenosyl methionine (SAM) cofactor analogues is described. A solvent-exposed channel present in the SAM-forming enzyme SalL tolerates 5'-chloro-5'-deoxyadenosine (ClDA) analogues modified at the 2-position of the adenine nucleobase. Coupling SalL-catalyzed cofactor production with C-(m)ethyl transfer to coumarin substrates catalyzed by the methyltransferase (MTase) NovO forms C-(m)ethylated coumarins in superior yield and greater substrate scope relative to that obtained using cofactors lacking nucleobase modifications. Establishing the molecular determinants that influence C-alkylation provides the basis to develop a late-stage enzymatic platform for the preparation of high value small molecules. | ||
| - | + | S-Adenosyl Methionine Cofactor Modifications Enhance the Biocatalytic Repertoire of Small Molecule C-Alkylation.,McKean IJW, Sadler JC, Cuetos A, Frese A, Humphreys LD, Grogan G, Hoskisson PA, Burley GA Angew Chem Int Ed Engl. 2019 Dec 2;58(49):17583-17588. doi:, 10.1002/anie.201908681. Epub 2019 Oct 21. PMID:31573135<ref>PMID:31573135</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6rz2" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Grogan | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Salinispora tropica CNB-440]] | ||
| + | [[Category: Burley G]] | ||
| + | [[Category: Cuetos A]] | ||
| + | [[Category: Frese A]] | ||
| + | [[Category: Grogan G]] | ||
| + | [[Category: McKean I]] | ||
Current revision
SalL with Chloroadenosine
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