2M5J

Solution structure of the periplasmic signaling domain of HasR, a TonB-dependent outer membrane heme transporter

2M5J の概要

• エントリーDOI: 10.2210/pdb2m5j/pdb
• 関連するPDBエントリー: 3CSL 3CSN 3DDR
• NMR情報: BMRB: 18201
• 分子名称: HasR protein (1 entity in total)
• 機能のキーワード: signaling domain, tonb dependent transporter, signaling protein
• 由来する生物種: Serratia marcescens (Serratia marcescens)
• 細胞内の位置: Cell outer membrane (By similarity): Q79AD2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11106.59

構造登録者

Malki, I.,Cardoso de Amorim, G.,Prochnicka-Chalufour, A.,Simenel, C.,Delepierre, M.,Izadi-Pruneyre, N. (登録日: 2013-02-26, 公開日: 2014-03-05, 最終更新日: 2024-05-15)

主引用文献

Malki, I.,Simenel, C.,Wojtowicz, H.,Cardoso de Amorim, G.,Prochnicka-Chalufour, A.,Hoos, S.,Raynal, B.,England, P.,Chaffotte, A.,Delepierre, M.,Delepelaire, P.,Izadi-Pruneyre, N.
Interaction of a Partially Disordered Antisigma Factor with Its Partner, the Signaling Domain of the TonB-Dependent Transporter HasR
Plos One, 9:e89502-e89502, 2014

PubMed Abstract: Bacteria use diverse signaling pathways to control gene expression in response to external stimuli. In Gram-negative bacteria, the binding of a nutrient is sensed by an outer membrane transporter. This signal is then transmitted to an antisigma factor and subsequently to the cytoplasm where an ECF sigma factor induces expression of genes related to the acquisition of this nutrient. The molecular interactions involved in this transmembrane signaling are poorly understood and structural data on this family of antisigma factor are rare. Here, we present the first structural study of the periplasmic domain of an antisigma factor and its interaction with the transporter. The study concerns the signaling in the heme acquisition system (Has) of Serratia marcescens. Our data support unprecedented partially disordered periplasmic domain of an anti-sigma factor HasS in contact with a membrane-mimicking environment. We solved the 3D structure of the signaling domain of HasR transporter and identified the residues at the HasS-HasR interface. Their conservation in several bacteria suggests wider significance of the proposed model for the understanding of bacterial transmembrane signaling.

PubMed: 24727671
DOI: 10.1371/journal.pone.0089502

実験手法

SOLUTION NMR