4RBT

PduA K26A S40L mutant, from Salmonella enterica serovar Typhimurium LT2

4RBT の概要

• エントリーDOI: 10.2210/pdb4rbt/pdb
• 関連するPDBエントリー: 4RBU 4RBV
• 分子名称: Propanediol utilization protein PduA, SULFATE ION (3 entities in total)
• 機能のキーワード: bacterial microcompartment shell protein, structural protein
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 31299.11

構造登録者

Chun, S.,Sawaya, M.R.,Yeates, T.O. (登録日: 2014-09-12, 公開日: 2015-02-18, 最終更新日: 2023-09-20)

主引用文献

Chowdhury, C.,Chun, S.,Pang, A.,Sawaya, M.R.,Sinha, S.,Yeates, T.O.,Bobik, T.A.
Selective molecular transport through the protein shell of a bacterial microcompartment organelle.
Proc.Natl.Acad.Sci.USA, 112:2990-2995, 2015

PubMed Abstract: Bacterial microcompartments are widespread prokaryotic organelles that have important and diverse roles ranging from carbon fixation to enteric pathogenesis. Current models for microcompartment function propose that their outer protein shell is selectively permeable to small molecules, but whether a protein shell can mediate selective permeability and how this occurs are unresolved questions. Here, biochemical and physiological studies of structure-guided mutants are used to show that the hexameric PduA shell protein of the 1,2-propanediol utilization (Pdu) microcompartment forms a selectively permeable pore tailored for the influx of 1,2-propanediol (the substrate of the Pdu microcompartment) while restricting the efflux of propionaldehyde, a toxic intermediate of 1,2-propanediol catabolism. Crystal structures of various PduA mutants provide a foundation for interpreting the observed biochemical and phenotypic data in terms of molecular diffusion across the shell. Overall, these studies provide a basis for understanding a class of selectively permeable channels formed by nonmembrane proteins.

PubMed: 25713376
DOI: 10.1073/pnas.1423672112

実験手法

X-RAY DIFFRACTION (2.3 Å)