2M2K

The structure of HasB CTD

2M2K の概要

• エントリーDOI: 10.2210/pdb2m2k/pdb
• NMR情報: BMRB: 15440
• 分子名称: HasB protein (1 entity in total)
• 機能のキーワード: hasb ctd, tonb-like protein, hemophore, heme acquisition system, transport protein
• 由来する生物種: Serratia marcescens
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14294.27

構造登録者

Prochnicka-Chalufour, A.,Lefevre, J.,Simenel, C.,Delepelaire, P.,Wandersman, C.,Delepierre, M.,Izadi-Pruneyre, N. (登録日: 2012-12-26, 公開日: 2013-04-10, 最終更新日: 2024-05-15)

主引用文献

de Amorim, G.C.,Prochnicka-Chalufour, A.,Delepelaire, P.,Lefevre, J.,Simenel, C.,Wandersman, C.,Delepierre, M.,Izadi-Pruneyre, N.
The Structure of HasB Reveals a New Class of TonB Protein Fold.
Plos One, 8:e58964-e58964, 2013

PubMed Abstract: TonB is a key protein in active transport of essential nutrients like vitamin B12 and metal sources through the outer membrane transporters of Gram-negative bacteria. This inner membrane protein spans the periplasm, contacts the outer membrane receptor by its periplasmic domain and transduces energy from the cytoplasmic membrane pmf to the receptor allowing nutrient internalization. Whereas generally a single TonB protein allows the acquisition of several nutrients through their cognate receptor, in some species one particular TonB is dedicated to a specific system. Despite a considerable amount of data available, the molecular mechanism of TonB-dependent active transport is still poorly understood. In this work, we present a structural study of a TonB-like protein, HasB dedicated to the HasR receptor. HasR acquires heme either free or via an extracellular heme transporter, the hemophore HasA. Heme is used as an iron source by bacteria. We have solved the structure of the HasB periplasmic domain of Serratia marcescens and describe its interaction with a critical region of HasR. Some important differences are observed between HasB and TonB structures. The HasB fold reveals a new structural class of TonB-like proteins. Furthermore, we have identified the structural features that explain the functional specificity of HasB. These results give a new insight into the molecular mechanism of nutrient active transport through the bacterial outer membrane and present the first detailed structural study of a specific TonB-like protein and its interaction with the receptor.

PubMed: 23527057
DOI: 10.1371/journal.pone.0058964

実験手法

SOLUTION NMR