2hu9

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 2hu9, resolution 1.780Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

X-ray structure of the Archaeoglobus fulgidus CopZ N-terminal Domain

Overview

Bacterial CopZ proteins deliver copper to P1B-type Cu+-ATPases that are, homologous to the human Wilson and Menkes disease proteins. The genome of, the hyperthermophile Archaeoglobus fulgidus encodes a putative CopZ copper, chaperone that contains an unusual cysteine-rich N-terminal domain of 130, amino acids in addition to a C-terminal copper binding domain with a, conserved CXXC motif. The N-terminal domain (CopZ-NT) is homologous to, proteins found only in extremophiles and is the only such protein that is, fused to a copper chaperone. Surprisingly, optical, electron paramagnetic, resonance, and x-ray absorption spectroscopic data indicate the presence, of a [2Fe-2S] cluster in CopZ-NT. The intact CopZ protein binds two copper, ions, one in each domain. The 1.8 A resolution crystal structure of, CopZ-NT reveals that the [2Fe-2S] cluster is housed within a novel fold, and that the protein also binds a zinc ion at a four-cysteine site. CopZ, can deliver Cu+ to the A. fulgidus CopA N-terminal metal binding domain, and is capable of reducing Cu2+ to Cu+. This unique fusion of a, redox-active domain with a CXXC-containing copper chaperone domain is, relevant to the evolution of copper homeostatic mechanisms and suggests, new models for copper trafficking.

About this Structure

2HU9 is a Single protein structure of sequence from Archaeoglobus fulgidus with , and as ligands. Full crystallographic information is available from OCA.

Reference

Characterization and structure of a Zn2+ and [2Fe-2S]-containing copper chaperone from Archaeoglobus fulgidus., Sazinsky MH, LeMoine B, Orofino M, Davydov R, Bencze KZ, Stemmler TL, Hoffman BM, Arguello JM, Rosenzweig AC, J Biol Chem. 2007 Aug 31;282(35):25950-9. Epub 2007 Jul 3. PMID:17609202

Page seeded by OCA on Wed Jan 23 12:48:54 2008