4XKP
Crystal structure of NikA from Staphylococcus aureus in complex with Ni(L-His)2 (co-crystallization with Ni(II) and BHI medium supernatant)
Summary for 4XKP
| Entry DOI | 10.2210/pdb4xkp/pdb |
| Related | 4OFJ 4XKN 4XKQ 4XKR |
| Descriptor | Nickel ABC transporter substrate-binding protein, NICKEL (II) ION, HISTIDINE, ... (6 entities in total) |
| Functional Keywords | extracytoplasmic nickel-binding protein, nickel import, abc-type importer, transport protein |
| Biological source | Staphylococcus aureus USA300-ISMMS1 |
| Total number of polymer chains | 1 |
| Total formula weight | 54983.45 |
| Authors | Lebrette, H.,Cavazza, C. (deposition date: 2015-01-12, release date: 2015-02-11, Last modification date: 2024-01-10) |
| Primary citation | Lebrette, H.,Borezee-Durant, E.,Martin, L.,Richaud, P.,Boeri Erba, E.,Cavazza, C. Novel insights into nickel import in Staphylococcus aureus: the positive role of free histidine and structural characterization of a new thiazolidine-type nickel chelator. Metallomics, 7:613-621, 2015 Cited by PubMed Abstract: Staphylococcus 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. PubMed: 25611161DOI: 10.1039/c4mt00295d PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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