4XKP

Crystal structure of NikA from Staphylococcus aureus in complex with Ni(L-His)2 (co-crystallization with Ni(II) and BHI medium supernatant)

4XKP の概要

• エントリーDOI: 10.2210/pdb4xkp/pdb
• 関連するPDBエントリー: 4OFJ 4XKN 4XKQ 4XKR
• 分子名称: Nickel ABC transporter substrate-binding protein, NICKEL (II) ION, HISTIDINE, ... (6 entities in total)
• 機能のキーワード: extracytoplasmic nickel-binding protein, nickel import, abc-type importer, transport protein
• 由来する生物種: Staphylococcus aureus USA300-ISMMS1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54983.45

構造登録者

Lebrette, H.,Cavazza, C. (登録日: 2015-01-12, 公開日: 2015-02-11, 最終更新日: 2024-01-10)

主引用文献

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

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: 25611161
DOI: 10.1039/c4mt00295d

実験手法

X-RAY DIFFRACTION (1.9 Å)