5vd6
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a GNAT superfamily acetyltransferase PA4794 in complex with bisubstrate analog 6== | |
| + | <StructureSection load='5vd6' size='340' side='right' caption='[[5vd6]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5vd6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VD6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VD6 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=93P:(3R,5S,9R,23S)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-10,14-dioxo-23-({[(phenylacetyl)amino]acetyl}amino)-2,4,6-trioxa-18-thia-11,15-diaza-3,5-diphosphatetracosan-24-oic+acid+3,5-dioxide+(non-preferred+name)'>93P</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l8a|4l8a]], [[5vdb|5vdb]]</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=5vd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vd6 OCA], [http://pdbe.org/5vd6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vd6 RCSB], [http://www.ebi.ac.uk/pdbsum/5vd6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vd6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Gcn5-related N-acetyltransferases (GNATs) are found in all kingdoms of life and catalyze important acyl transfer reactions in diverse cellular processes. While many 3D structures of GNATs have been determined, most do not contain acceptor substrates in their active sites. To expand upon existing crystallographic strategies for improving acceptor-bound GNAT structures, we synthesized peptide substrate analogs and reacted them with CoA in PA4794 protein crystals. We found two separate mechanisms for bisubstrate formation: (a) a novel X-ray induced radical-mediated alkylation of CoA with an alkene peptide and (b) direct alkylation of CoA with a halogenated peptide. Our approach is widely applicable across the GNAT superfamily and can be used to improve the success rate of obtaining liganded structures of other acyltransferases. | ||
| - | + | Generating enzyme and radical-mediated bisubstrates as tools for investigating Gcn5-related N-acetyltransferases.,Reidl C, Majorek KA, Dang J, Tran D, Jew K, Law M, Payne Y, Minor W, Becker DP, Kuhn ML FEBS Lett. 2017 Aug;591(15):2348-2361. doi: 10.1002/1873-3468.12753. Epub 2017, Aug 1. PMID:28703494<ref>PMID:28703494</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 5vd6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Joachimiak, A]] | [[Category: Joachimiak, A]] | ||
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Majorek, K A]] |
[[Category: Minor, W]] | [[Category: Minor, W]] | ||
| + | [[Category: Acetyltransferase]] | ||
| + | [[Category: Bisubstrate inhibitor]] | ||
| + | [[Category: Gnat]] | ||
| + | [[Category: Mcsg]] | ||
| + | [[Category: Psi-biology]] | ||
| + | [[Category: Transferase]] | ||
| + | [[Category: Transferase-transferase inhibitor complex]] | ||
Revision as of 10:58, 24 August 2017
Crystal structure of a GNAT superfamily acetyltransferase PA4794 in complex with bisubstrate analog 6
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