2ldi | pdb_00002ldi

NMR solution structure of ZiaAN sub mutant

spinqualitylabelsall models 2ldi, 30 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ldi is a 1 chain structure with sequence from Aphanocapsa sp. (strain n-1). Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2ofg, 2ofh Gene: ziaA, slr0798 (Aphanocapsa sp. (strain N-1)) Activity: Zinc-exporting ATPase, with EC number 3.6.3.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed 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, Deltaatx1DeltagshB are hypersensitive to elevated copper relative to wild type cells and also relative to DeltagshB 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. Cyanobacterial metallochaperone inhibits deleterious side reactions of copper.,Tottey S, Patterson CJ, Banci L, Bertini I, Felli IC, Pavelkova A, Dainty SJ, Pernil R, Waldron KJ, Foster AW, Robinson NJ Proc Natl Acad Sci U S A. 2012 Jan 3;109(1):95-100. Epub 2011 Dec 22. PMID:22198771 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA