8ad8

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'''Unreleased structure'''
 
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The entry 8ad8 is ON HOLD until Paper Publication
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==Flavin-dependent tryptophan 6-halogenase Thal in complex with a D-Trp-Ser dipeptide==
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<StructureSection load='8ad8' size='340' side='right'caption='[[8ad8]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8ad8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_albogriseolus Streptomyces albogriseolus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AD8 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LT0:D-tryptophyl-L-serine'>LT0</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ad8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ad8 OCA], [https://pdbe.org/8ad8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ad8 RCSB], [https://www.ebi.ac.uk/pdbsum/8ad8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ad8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A1E280_STRAO A1E280_STRAO]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The late-stage site-selective derivatisation of peptides has many potential applications in structure-activity relationship studies and postsynthetic modification or conjugation of bioactive compounds. The development of orthogonal methods for C-H functionalisation is crucial for such peptide derivatisation. Among them biocatalytic methods are increasingly attracting attention. Tryptophan halogenases emerged as valuable catalysts to functionalise tryptophan (Trp), while direct enzyme-catalysed halogenation of synthetic peptides is yet unprecedented. Here, it is reported that the Trp 6-halogenase Thal accepts a wide range of amides and peptides containing a Trp moiety. Increasing the sequence length and reaction optimisation made bromination of pentapeptides feasible with good turnovers and a broad sequence scope, while regioselectivity turned out to be sequence dependent. Comparison of X-ray single crystal structures of Thal in complex with d-Trp and a dipeptide revealed a significantly altered binding mode for the peptide. The viability of this bioorthogonal approach was exemplified by halogenation of a cyclic RGD peptide.
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Authors:
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Enzymatic Late-Stage Halogenation of Peptides.,Schnepel C, Moritzer AC, Gafe S, Montua N, Minges H, Niess A, Niemann HH, Sewald N Chembiochem. 2022 Oct 19. doi: 10.1002/cbic.202200569. PMID:36259362<ref>PMID:36259362</ref>
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Description:
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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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<div class="pdbe-citations 8ad8" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Streptomyces albogriseolus]]
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[[Category: Gaefe S]]
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[[Category: Montua N]]
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[[Category: Moritzer AC]]
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[[Category: Niemann HH]]
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[[Category: Sewald N]]

Revision as of 07:36, 3 November 2022

Flavin-dependent tryptophan 6-halogenase Thal in complex with a D-Trp-Ser dipeptide

PDB ID 8ad8

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