7Q1G

Crystal structure and metal binding properties of the periplasmic iron component EfeM from Pseudomonas syringae EfeUOB/M iron-transport system

「6SNG」から置き換えられました 「4BGO」から置き換えられました

7Q1G の概要

• エントリーDOI: 10.2210/pdb7q1g/pdb
• 分子名称: Peptidase_M75 domain-containing protein, SULFATE ION (3 entities in total)
• 機能のキーワード: efem, peptidase-m75 domain, metal-binding, efeuob iron-transport system, metal transport
• 由来する生物種: Pseudomonas syringae pv. syringae (strain B728a)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64038.06

構造登録者

Watson, K.A.,Rajasekaran, M. (登録日: 2021-10-19, 公開日: 2022-04-27, 最終更新日: 2024-01-31)

主引用文献

Rajasekaran, M.B.,Hussain, R.,Siligardi, G.,Andrews, S.C.,Watson, K.A.
Crystal structure and metal binding properties of the periplasmic iron component EfeM from Pseudomonas syringae EfeUOB/M iron-transport system.
Biometals, 35:573-589, 2022

PubMed Abstract: EfeUOB/M has been characterised in Pseudomonas syringae pathovar. syringae as a novel type of ferrous-iron transporter, consisting of an inner-membrane protein (EfeU) and three periplasmic proteins (EfeO, EfeM and EfeB). The role of an iron permease and peroxidase function has been identified for the EfeU and EfeB proteins, respectively, but the role of EfeO/M remains unclear. EfeM is an 'M75-only' EfeO-like protein with a C-terminal peptidase-M75 domain (EfeO/EfeM family). Herein, we report the 1.6 Å resolution crystal structure of EfeM, the first structural report for an EfeM component of P. syringae pv. syringae. The structure possesses the bi-lobate architecture found in other bacterial periplasmic substrate/solute binding proteins. Metal binding studies, using SRCD and ICP-OES, reveal a preference of EfeM for copper, iron and zinc. This work provides detailed knowledge of the structural scaffold, the metal site geometry, and the divalent metal binding potential of EfeM. This work provides crucial underpinning for a more detailed understanding of the role of EfeM/EfeO proteins and the peptidase-M75 domains in EfeUOB/M iron uptake systems in bacteria.

PubMed: 35348940
DOI: 10.1007/s10534-022-00389-2

実験手法

X-RAY DIFFRACTION (1.6 Å)