5VD6

Crystal structure of a GNAT superfamily acetyltransferase PA4794 in complex with bisubstrate analog 6

5VD6 の概要

• エントリーDOI: 10.2210/pdb5vd6/pdb
• 関連するPDBエントリー: 4L8A 5VDB
• 分子名称: acetyltransferase PA4794, SULFATE ION, (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), ... (4 entities in total)
• 機能のキーワード: gnat, acetyltransferase, bisubstrate inhibitor, structural genomics, psi-biology, midwest center for structural genomics, mcsg, transferase, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• 由来する生物種: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19648.85

構造登録者

Majorek, K.A.,Joachimiak, A.,Minor, W.,Midwest Center for Structural Genomics (MCSG) (登録日: 2017-04-01, 公開日: 2017-07-26, 最終更新日: 2023-10-04)

主引用文献

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

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: 28703494
DOI: 10.1002/1873-3468.12753

実験手法

X-RAY DIFFRACTION (1.2 Å)