7LB6

PDX1.2/PDX1.3 co-expression complex

7LB6 の概要

• エントリーDOI: 10.2210/pdb7lb6/pdb
• EMDBエントリー: 23263 23264
• 分子名称: Pyridoxal 5'-phosphate synthase-like subunit PDX1.2, Pyridoxal 5'-phosphate synthase subunit PDX1.3 (2 entities in total)
• 機能のキーワード: pseudoenzyme, dodecamer, vitamin b6, plant protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress); 詳細
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 886602.42

構造登録者

Novikova, I.V.,Evans, J.E. (登録日: 2021-01-07, 公開日: 2021-09-22, 最終更新日: 2024-05-29)

主引用文献

Novikova, I.V.,Zhou, M.,Du, C.,Parra, M.,Kim, D.N.,VanAernum, Z.L.,Shaw, J.B.,Hellmann, H.,Wysocki, V.H.,Evans, J.E.
Tunable Heteroassembly of a Plant Pseudoenzyme-Enzyme Complex.
Acs Chem.Biol., 16:2315-2325, 2021

PubMed Abstract: Pseudoenzymes have emerged as key regulatory elements in all kingdoms of life despite being catalytically nonactive. Yet many factors defining why one protein is active while its homologue is inactive remain uncertain. For pseudoenzyme-enzyme pairs, the similarity of both subunits can often hinder conventional characterization approaches. In plants, a pseudoenzyme, PDX1.2, positively regulates vitamin B production by association with its active catalytic homologues such as PDX1.3 through an unknown assembly mechanism. Here we used an integrative experimental approach to learn that such pseudoenzyme-enzyme pair associations result in heterocomplexes of variable stoichiometry, which are unexpectedly tunable. We also present the atomic structure of the PDX1.2 pseudoenzyme as well as the population averaged PDX1.2-PDX1.3 pseudoenzyme-enzyme pair. Finally, we dissected hetero-dodecamers of each stoichiometry to understand the arrangement of monomers in the heterocomplexes and identified symmetry-imposed preferences in PDX1.2-PDX1.3 interactions. Our results provide a new model of pseudoenzyme-enzyme interactions and their native heterogeneity.

PubMed: 34520180
DOI: 10.1021/acschembio.1c00475

実験手法

ELECTRON MICROSCOPY (3.16 Å)