6S4G

Crystal structure of the omega transaminase from Chromobacterium violaceum in complex with PMP

6S4G の概要

• エントリーDOI: 10.2210/pdb6s4g/pdb
• 分子名称: Probable aminotransferase, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: transaminase, pmp, plp-dependent enzyme, complex, transferase
• 由来する生物種: Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 209947.98

構造登録者

Ruggieri, F.,Campillo Brocal, J.C.,Humble, M.S.,Walse, B.,Logan, D.T.,Berglund, P. (登録日: 2019-06-27, 公開日: 2019-07-17, 最終更新日: 2024-01-24)

主引用文献

Ruggieri, F.,Campillo-Brocal, J.C.,Chen, S.,Humble, M.S.,Walse, B.,Logan, D.T.,Berglund, P.
Insight into the dimer dissociation process of the Chromobacterium violaceum (S)-selective amine transaminase.
Sci Rep, 9:16946-16946, 2019

PubMed Abstract: One of the main factors hampering the implementation in industry of transaminase-based processes for the synthesis of enantiopure amines is their often low storage and operational stability. Our still limited understanding of the inactivation processes undermining the stability of wild-type transaminases represents an obstacle to improving their stability through enzyme engineering. In this paper we present a model describing the inactivation process of the well-characterized (S)-selective amine transaminase from Chromobacterium violaceum. The cornerstone of the model, supported by structural, computational, mutagenesis and biophysical data, is the central role of the catalytic lysine as a conformational switch. Upon breakage of the lysine-PLP Schiff base, the strain associated with the catalytically active lysine conformation is dissipated in a slow relaxation process capable of triggering the known structural rearrangements occurring in the holo-to-apo transition and ultimately promoting dimer dissociation. Due to the occurrence in the literature of similar PLP-dependent inactivation models valid for other non-transaminase enzymes belonging to the same fold-class, the role of the catalytic lysine as conformational switch might extend beyond the transaminase enzyme group and offer new insight to drive future non-trivial engineering strategies.

PubMed: 31740704
DOI: 10.1038/s41598-019-53177-3

実験手法

X-RAY DIFFRACTION (1.67 Å)