2m5j

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

spinqualitylabelsall models 2m5j Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2m5j is a 1 chain structure with sequence from Serratia marcescens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q79AD2_SERMA Publication Abstract from PubMed 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. Interaction of a Partially Disordered Antisigma Factor with Its Partner, the Signaling Domain of the TonB-Dependent Transporter HasR.,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 PLoS One. 2014 Apr 11;9(4):e89502. doi: 10.1371/journal.pone.0089502. eCollection, 2014. PMID:24727671 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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