4i8c
X-ray structure of NikA in complex with Ni-(L-His)2X-ray structure of NikA in complex with Ni-(L-His)2
Structural highlights
Function[NIKA_ECOLI] Involved in a nickel transport system, probably represents the nickel binder. Publication Abstract from PubMedThe ABC-type importer NikABCDE mediates nickel acquisition in Escherichia coli. The periplasmic nickel-binding component NikA has a folding similar to that of the peptide transporter OppA and does not bind free nickel. Instead, we showed that the metal is tetra-coordinated by an organic tri-dentate molecule and His416. Conversely, it has been recently reported that NikA binds Ni-((L)-His)(2) and that addition of histidine increases the rate of nickel uptake in vivo. Here, we report the structure of NikA/Ni-((L)-His)(2) and show that histidine binding differs from peptide binding in OppA. The structure also confirms the central role of His416 in nickel binding. The binding mode of Ni-((L)-His)(2) in NikA revealed by X-ray crystallography.,Lebrette H, Iannello M, Fontecilla-Camps JC, Cavazza C J Inorg Biochem. 2012 Dec 23;121C:16-18. doi: 10.1016/j.jinorgbio.2012.12.010. PMID:23314594[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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