2M5J
Solution structure of the periplasmic signaling domain of HasR, a TonB-dependent outer membrane heme transporter
Summary for 2M5J
| Entry DOI | 10.2210/pdb2m5j/pdb |
| Related | 3CSL 3CSN 3DDR |
| NMR Information | BMRB: 18201 |
| Descriptor | HasR protein (1 entity in total) |
| Functional Keywords | signaling domain, tonb dependent transporter, signaling protein |
| Biological source | Serratia marcescens (Serratia marcescens) |
| Cellular location | Cell outer membrane (By similarity): Q79AD2 |
| Total number of polymer chains | 1 |
| Total formula weight | 11106.59 |
| Authors | Malki, I.,Cardoso de Amorim, G.,Prochnicka-Chalufour, A.,Simenel, C.,Delepierre, M.,Izadi-Pruneyre, N. (deposition date: 2013-02-26, release date: 2014-03-05, Last modification date: 2024-05-15) |
| Primary citation | 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 Cited by 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: 24727671DOI: 10.1371/journal.pone.0089502 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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