8CBB

Structure of homodimeric luciferase from Enhygromyxa salina

8CBB の概要

• エントリーDOI: 10.2210/pdb8cbb/pdb
• 分子名称: Alkanal monooxygenase alpha chain, SULFATE ION (3 entities in total)
• 機能のキーワード: luciferase, monooxygenase, luminescent protein
• 由来する生物種: Enhygromyxa salina
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 169488.25

構造登録者

Yudenko, A.,Remeeva, A.,Gushchin, I. (登録日: 2023-01-25, 公開日: 2024-02-07, 最終更新日: 2024-11-20)

主引用文献

Yudenko, A.,Bazhenov, S.V.,Aleksenko, V.A.,Goncharov, I.M.,Semenov, O.,Remeeva, A.,Nazarenko, V.V.,Kuznetsova, E.,Fomin, V.V.,Konopleva, M.N.,Al Ebrahim, R.,Sluchanko, N.N.,Ryzhykau, Y.,Semenov, Y.S.,Kuklin, A.,Manukhov, I.V.,Gushchin, I.
luxA Gene From Enhygromyxa salina Encodes a Functional Homodimeric Luciferase.
Proteins, 92:1449-1458, 2024

PubMed Abstract: Several clades of luminescent bacteria are known currently. They all contain similar lux operons, which include the genes luxA and luxB encoding a heterodimeric luciferase. The aldehyde oxygenation reaction is presumed to be catalyzed primarily by the subunit LuxA, whereas LuxB is required for efficiency and stability of the complex. Recently, genomic analysis identified a subset of bacterial species with rearranged lux operons lacking luxB. Here, we show that the product of the luxA gene from the reduced luxACDE operon of Enhygromyxa salina is luminescent upon addition of aldehydes both in vivo in Escherichia coli and in vitro. Overall, EsLuxA is much less bright compared with luciferases from Aliivibrio fischeri (AfLuxAB) and Photorhabdus luminescens (PlLuxAB), and most active with medium-chain C4-C9 aldehydes. Crystal structure of EsLuxA determined at the resolution of 2.71 Å reveals a (β/α) TIM-barrel fold, characteristic for other bacterial luciferases, and the protein preferentially forms a dimer in solution. The mobile loop residues 264-293, which form a β-hairpin or a coil in Vibrio harveyi LuxA, form α-helices in EsLuxA. Phylogenetic analysis shows EsLuxA and related proteins may be bacterial protoluciferases that arose prior to duplication of the luxA gene and its speciation to luxA and luxB in the previously described luminescent bacteria. Our work paves the way for the development of new bacterial luciferases that have an advantage of being encoded by a single gene.

PubMed: 39171358
DOI: 10.1002/prot.26739

実験手法

X-RAY DIFFRACTION (2.71 Å)