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Crystal structure of NikA from Staphylococcus aureus in complex with Ni(L-His)2
Structural highlights
FunctionNIKA_STAA8 Part of the ABC transporter complex NikABCDE (Opp2) involved in nickel import. Binds nickel and transfers it to the membrane-bound permease. Required for full urease activity and plays a significant role in the virulence of S.aureus during urinary tract infection (UTI) (PubMed:20662775). May bind nickel via a nickel-chelator (PubMed:25611161).[1] [2] Publication Abstract from PubMedStaphylococcus aureus possesses two canonical ABC-importers dedicated to nickel acquisition: the NikABCDE and the CntABCDF systems, active under different growth conditions. This study reports on the extracytoplasmic nickel-binding components SaNikA and SaCntA. We showed by protein crystallography that SaNikA is able to bind either a Ni-(l-His)2 complex or a Ni-(l-His) (2-methyl-thiazolidine dicarboxylate) complex, depending on their availability in culture supernatants. Native mass spectrometry experiments on SaCntA revealed that it binds the Ni(ii) ion via a different histidine-dependent chelator but it cannot bind Ni-(l-His)2. In vitro experiments are consistent with in vivo nickel content measurements that showed that l-histidine has a high positive impact on nickel import via the Cnt system. These results suggest that although both systems may require free histidine, they use different strategies to import nickel. Novel insights into nickel import in Staphylococcus aureus: the positive role of free histidine and structural characterization of a new thiazolidine-type nickel chelator.,Lebrette H, Borezee-Durant E, Martin L, Richaud P, Boeri Erba E, Cavazza C Metallomics. 2015 Jan 22. PMID:25611161[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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