PDBsum entry 4xkp

Transport protein

PDB id: 4xkp

Contents

Protein chain

465 a.a.

Ligands

HIS ×2

GOL ×9

EPE

Metals

_NI

Waters ×415

PDB id:

4xkp

Name:

Transport protein

Title:

Crystal structure of nika from staphylococcus aureus in complex with ni(l-his)2 (co-crystallization with ni(ii) and bhi medium supernatant)

Structure:

Nickel abc transporter substrate-binding protein. Chain: a. Fragment: unp residues 19-491. Engineered: yes

Source:

Staphylococcus aureus usa300-ismms1. Organism_taxid: 1458279. Gene: az30_01190. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008

Resolution:

1.90Å R-factor: 0.160 R-free: 0.191

Authors:

H.Lebrette,C.Cavazza

Key ref:

H.Lebrette et al. (2015). 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. PubMed id: 25611161 DOI: 10.1039/c4mt00295d

Date:

12-Jan-15 Release date: 11-Feb-15

Protein chain

Q2G2P5  (Q2G2P5_STAA8) -  Nickel-binding protein NikA from Staphylococcus aureus (strain NCTC 8325 / PS 47)

Seq: 491 a.a.

Struc: 465 a.a.

DOI no: 10.1039/c4mt00295d

Metallomics 7:613-621 (2015)

PubMed id: 25611161

Novel insights into nickel import in Staphylococcus aureus: the positive role of free histidine and structural characterization of a new thiazolidine-type nickel chelator.

H.Lebrette, E.Borezée-Durant, L.Martin, P.Richaud, E.Boeri Erba, C.Cavazza.

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.