2LDI

NMR solution structure of ZiaAN sub mutant

Summary for 2LDI

• Entry DOI: 10.2210/pdb2ldi/pdb
• Related: 2OFG 2OFH
• NMR Information: BMRB: 17668
• Descriptor: Zinc-transporting ATPase (1 entity in total)
• Functional Keywords: metal homeostasis, metallochaperones, hydrolase
• Biological source: Synechocystis sp. PCC 6803 substr. Kazusa
• Cellular location: Cell membrane; Multi-pass membrane protein: Q59998
• Total number of polymer chains: 1
• Total formula weight: 11489.97

Authors

Banci, L.,Bertini, I.,Felli, I.C.,Pavelkova, A. (deposition date: 2011-05-26, release date: 2011-11-30, Last modification date: 2024-05-15)

Primary citation

Tottey, S.,Patterson, C.J.,Banci, L.,Bertini, I.,Felli, I.C.,Pavelkova, A.,Dainty, S.J.,Pernil, R.,Waldron, K.J.,Foster, A.W.,Robinson, N.J.
Cyanobacterial metallochaperone inhibits deleterious side reactions of copper.
Proc.Natl.Acad.Sci.USA, 109:95-100, 2012

PubMed Abstract: Copper metallochaperones supply copper to cupro-proteins through copper-mediated protein-protein-interactions and it has been hypothesized that metallochaperones thereby inhibit copper from causing damage en route. Evidence is presented in support of this latter role for cyanobacterial metallochaperone, Atx1. In cyanobacteria Atx1 contributes towards the supply of copper to plastocyanin inside thylakoids but it is shown here that in copper-replete medium, copper can reach plastocyanin without Atx1. Unlike metallochaperone-independent copper-supply to superoxide dismutase in eukaryotes, glutathione is not essential for Atx1-independent supply to plastocyanin: Double mutants missing atx1 and gshB (encoding glutathione synthetase) accumulate the same number of atoms of copper per cell in the plastocyanin pool as wild type. Critically, Δatx1ΔgshB are hypersensitive to elevated copper relative to wild type cells and also relative to ΔgshB single mutants with evidence that hypersensitivity arises due to the mislocation of copper to sites for other metals including iron and zinc. The zinc site on the amino-terminal domain (ZiaA(N)) of the P(1)-type zinc-transporting ATPase is especially similar to the copper site of the Atx1 target PacS(N), and ZiaA(N) will bind Cu(I) more tightly than zinc. An NMR model of a substituted-ZiaA(N)-Cu(I)-Atx1 heterodimer has been generated making it possible to visualize a juxtaposition of residues surrounding the ZiaA(N) zinc site, including Asp(18), which normally repulse Atx1. Equivalent repulsion between bacterial copper metallochaperones and the amino-terminal regions of P(1)-type ATPases for metals other than Cu(I) is conserved, again consistent with a role for copper metallochaperones to withhold copper from binding sites for other metals.

PubMed: 22198771
DOI: 10.1073/pnas.1117515109

Experimental method

SOLUTION NMR