5D79

Structure of BBE-like #28 from Arabidopsis thaliana

5D79 の概要

• エントリーDOI: 10.2210/pdb5d79/pdb
• 分子名称: Berberine bridge enzyme-like protein, CHLORIDE ION, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: covalent fad binding, berberine bridge enzyme like, plant enzyme, oxidoreductase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• 細胞内の位置: Secreted, cell wall : Q9FI21
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 122257.06

構造登録者

Daniel, B.,Kumar, P.,Gruber, K. (登録日: 2015-08-13, 公開日: 2016-06-22, 最終更新日: 2024-11-13)

主引用文献

Daniel, B.,Wallner, S.,Steiner, B.,Oberdorfer, G.,Kumar, P.,van der Graaff, E.,Roitsch, T.,Sensen, C.W.,Gruber, K.,Macheroux, P.
Structure of a Berberine Bridge Enzyme-Like Enzyme with an Active Site Specific to the Plant Family Brassicaceae.
Plos One, 11:e0156892-e0156892, 2016

PubMed Abstract: Berberine bridge enzyme-like (BBE-like) proteins form a multigene family (pfam 08031), which is present in plants, fungi and bacteria. They adopt the vanillyl alcohol-oxidase fold and predominantly show bi-covalent tethering of the FAD cofactor to a cysteine and histidine residue, respectively. The Arabidopsis thaliana genome was recently shown to contain genes coding for 28 BBE-like proteins, while featuring four distinct active site compositions. We determined the structure of a member of the AtBBE-like protein family (termed AtBBE-like 28), which has an active site composition that has not been structurally and biochemically characterized thus far. The most salient and distinguishing features of the active site found in AtBBE-like 28 are a mono-covalent linkage of a histidine to the 8α-position of the flavin-isoalloxazine ring and the lack of a second covalent linkage to the 6-position, owing to the replacement of a cysteine with a histidine. In addition, the structure reveals the interaction of a glutamic acid (Glu426) with an aspartic acid (Asp369) at the active site, which appear to share a proton. This arrangement leads to the delocalization of a negative charge at the active site that may be exploited for catalysis. The structure also indicates a shift of the position of the isoalloxazine ring in comparison to other members of the BBE-like family. The dioxygen surrogate chloride was found near the C(4a) position of the isoalloxazine ring in the oxygen pocket, pointing to a rapid reoxidation of reduced enzyme by dioxygen. A T-DNA insertional mutant line for AtBBE-like 28 results in a phenotype, that is characterized by reduced biomass and lower salt stress tolerance. Multiple sequence analysis showed that the active site composition found in AtBBE-like 28 is only present in the Brassicaceae, suggesting that it plays a specific role in the metabolism of this plant family.

PubMed: 27276217
DOI: 10.1371/journal.pone.0156892

実験手法

X-RAY DIFFRACTION (1.849 Å)