3NGK

PduA from Salmonella enterica Typhimurium

3NGK の概要

• エントリーDOI: 10.2210/pdb3ngk/pdb
• 分子名称: Propanediol utilization protein pduA (2 entities in total)
• 機能のキーワード: bmc shell protein, pdu, carboxysome, propanediol, unknown function
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10591.19

構造登録者

Crowley, C.S.,Cascio, D.,Sawaya, M.R.,Yeates, T.O. (登録日: 2010-06-11, 公開日: 2010-10-06, 最終更新日: 2023-09-06)

主引用文献

Crowley, C.S.,Cascio, D.,Sawaya, M.R.,Kopstein, J.S.,Bobik, T.A.,Yeates, T.O.
Structural Insight into the Mechanisms of Transport across the Salmonella enterica Pdu Microcompartment Shell.
J.Biol.Chem., 285:37838-37846, 2010

PubMed Abstract: Bacterial microcompartments are a functionally diverse group of proteinaceous organelles that confine specific reaction pathways in the cell within a thin protein-based shell. The propanediol utilizing (Pdu) microcompartment contains the reactions for metabolizing 1,2-propanediol in certain enteric bacteria, including Salmonella. The Pdu shell is assembled from a few thousand protein subunits of several different types. Here we report the crystal structures of two key shell proteins, PduA and PduT. The crystal structures offer insights into the mechanisms of Pdu microcompartment assembly and molecular transport across the shell. PduA forms a symmetric homohexamer whose central pore appears tailored for facilitating transport of the 1,2-propanediol substrate. PduT is a novel, tandem domain shell protein that assembles as a pseudohexameric homotrimer. Its structure reveals an unexpected site for binding an [Fe-S] cluster at the center of the PduT pore. The location of a metal redox cofactor in the pore of a shell protein suggests a novel mechanism for either transferring redox equivalents across the shell or for regenerating luminal [Fe-S] clusters.

PubMed: 20870711
DOI: 10.1074/jbc.M110.160580

実験手法

X-RAY DIFFRACTION (2.2608 Å)