5VDB
Crystal structure of a GNAT superfamily acetyltransferase PA4794 in complex with bisubstrate analog 3
Summary for 5VDB
| Entry DOI | 10.2210/pdb5vdb/pdb |
| Related | 4L8A 5VD6 |
| Descriptor | acetyltransferase PA4794, SULFATE ION, (3R,5S,9R,26S)-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-10,14,20-trioxo-26-({[(phenylacetyl)amino]acetyl}amino)-2,4,6-trioxa-18-thia-11,15,21-triaza-3,5-diphosphaheptacosan-27-oic acid 3,5-dioxide (non-preferred name), ... (4 entities in total) |
| Functional Keywords | gnat, acetyltransferase, bisubstrate inhibitor, structural genomics, psi-biology, midwest center for structural genomics, mcsg, transferase, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Total number of polymer chains | 1 |
| Total formula weight | 19608.79 |
| Authors | Majorek, K.A.,Joachimiak, A.,Minor, W.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2017-04-01, release date: 2017-07-26, Last modification date: 2023-10-04) |
| Primary citation | Reidl, C.,Majorek, K.A.,Dang, J.,Tran, D.,Jew, K.,Law, M.,Payne, Y.,Minor, W.,Becker, D.P.,Kuhn, M.L. Generating enzyme and radical-mediated bisubstrates as tools for investigating Gcn5-related N-acetyltransferases. FEBS Lett., 591:2348-2361, 2017 Cited by PubMed Abstract: 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. PubMed: 28703494DOI: 10.1002/1873-3468.12753 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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