2HU9

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

Summary for 2HU9

• Entry DOI: 10.2210/pdb2hu9/pdb
• Descriptor: Mercuric transport protein periplasmic component, ZINC ION, FE2/S2 (INORGANIC) CLUSTER, ... (5 entities in total)
• Functional Keywords: copper chaperone, iron-sufur protein, copz, atx1, atox1, metal transport
• Biological source: Archaeoglobus fulgidus
• Cellular location: Cytoplasm (Probable): O29901
• Total number of polymer chains: 2
• Total formula weight: 30319.27

Authors

Sazinsky, M.H.,LeMoine, B.,Arguello, J.M.,Rosenzweig, A.C. (deposition date: 2006-07-26, release date: 2007-07-03, Last modification date: 2024-02-14)

Primary citation

Sazinsky, M.H.,LeMoine, B.,Orofino, M.,Davydov, R.,Bencze, K.Z.,Stemmler, T.L.,Hoffman, B.M.,Arguello, J.M.,Rosenzweig, A.C.
Characterization and structure of a Zn2+ and [2Fe-2S]-containing copper chaperone from Archaeoglobus fulgidus.
J.Biol.Chem., 282:25950-25959, 2007

PubMed Abstract: 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.

PubMed: 17609202
DOI: 10.1074/jbc.M703311200

Experimental method

X-RAY DIFFRACTION (1.78 Å)