5a4g

NMR structure of a 180 residue construct encompassing the N-terminal metal-binding site and the membrane proximal domain of SilB from Cupriavidus metallidurans CH34

spinqualitylabelsall models 5a4g Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a4g is a 1 chain structure with sequence from Cupriavidus metallidurans CH34. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: AG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q58AF3_CUPMC Publication Abstract from PubMed Silver ion resistance in bacteria mainly relies on efflux systems, and notably on tripartite efflux complexes involving a transporter from the resistance-nodulation-cell division (RND) superfamily, such as the SilCBA system from Cupriavidus metallidurans CH34. The periplasmic adaptor protein SilB hosts two specific metal coordination sites, located in the N-terminal and C-terminal domains, respectively, that are believed to play a different role in the efflux mechanism and the trafficking of metal ions from the periplasm to the RND transporter. On the basis of the known domain structure of periplasmic adaptor proteins, we designed different protein constructs derived from SilB domains with either one or two metal binding sites per protein chain. ITC data acquired on proteins with single metal sites suggest a slightly higher affinity of Ag(+) for the N-terminal metal site, compared to that for the C-terminal one. Remarkably, via the study of a protein construct featuring both metal sites, nuclear magnetic resonance (NMR) and fluorescence spectroscopies concordantly show that the C-terminal site is saturated prior to the N-terminal one. The C-terminal binding site is supposed to transfer the metal ions to the RND protein, while the transport driven by this latter is activated upon binding of the metal ion to the N-terminal site. Our results suggest that the filling of the C-terminal metal site is a key prerequisite for preventing futile activation of the transport system. Exhaustive NMR studies reveal for the first time the structure and dynamics of the functionally important N-terminal domain connected to the membrane proximal domain as well as of its Ag(+) binding site. Structural and Functional Investigation of the Ag(+)/Cu(+) Binding Domains of the Periplasmic Adaptor Protein SilB from Cupriavidus metallidurans CH34.,Urbina P, Bersch B, De Angelis F, Derfoufi KM, Prevost M, Goormaghtigh E, Vandenbussche G Biochemistry. 2016 May 24;55(20):2883-97. doi: 10.1021/acs.biochem.6b00022. Epub , 2016 May 13. PMID:27145046 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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