The X-ray structure of human serum ceruloplasmin at 3.1 Å: nature of the copper centres

Zaitseva, I. Ya.; Zaĭtsev, V. N.; Card, G.L.; Moshkov, K. A.; Bax, Benjamin; Ralph, Adam; Lindley, P. F.

doi:10.1007/s007750050018

Cited by 364 publications

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“…RT-PCRanalysis of our patient' s lymphoblasts indicated that mutant CP mRNAthat skipped exon 3 would be preferentially transcribed. Exon 3 encodes the latter half of domain 1 of the CP molecule, which includes Hisl61 and His163 indispensable for the binding of copper to its trinuclear center (19). Therefore, the mutant CP produced by this patient's hepatocytes would be structurally unstable and quickly degraded.…”

Section: Discussionmentioning

confidence: 99%

Aceruloplasminemia with Juvenile-onset Diabetes Mellitus Caused by Exon Skipping in the Ceruloplasmin Gene

Hatanaka¹,

Okano

Oda³

et al. 2003

Intern. Med.

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Weherein report a case of aceruloplasminemia in a 27-year-old man who had a 10-year history of diabetes mellitus. The patient developed a convulsion, most likely as a result of hypoglycemia. Unexpectedly, this episode left him in a prolonged state of unconsciousness, which necessitated neurological testing and imaging. Brain MRI showed bilateral hypo-intensities in the basal ganglia and thalamus. Molecular analysis revealed a novel splicing mutation in the ceruloplasmin (CP) gene that would result in the skipping of exon 3 during transcription. This case suggests that diabetes associated with aceruloplasminemia can becomemanifest in the teens. (Internal Medicine 42: 599-604, 2003)

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Section: Discussionmentioning

confidence: 99%

Aceruloplasminemia with Juvenile-onset Diabetes Mellitus Caused by Exon Skipping in the Ceruloplasmin Gene

Hatanaka¹,

Okano

Oda³

et al. 2003

Intern. Med.

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“…In some other cases, the protein does not provide any ligand residue at that position. For instance, a recently determined crystal structure of human ceruloplasmin reveals that one of the three blue copper sites in this multicopper oxidase is formed by only three equatorial ligands, two His and a Cys, while no residue has been found to contribute at its fourth, axial coordination position (Zaitseva et al, 1996). Similar to the ceruloplasmin, several fungal laccases (Xu et al, 1996) , and tobacco laccase as well (Kiefer-Meyer et al , 1996), possess nonliganding residues, such as Leu or Phe.…”

Section: Am Nersissian Et Almentioning

confidence: 99%

Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of phytocyanins: Plant‐specific mononuclear blue copper proteins

et al. 1998

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The cDNAs encoding plantacyanin from spinach were isolated and characterized. In addition, four new cDNA sequences from Arubidopsis ESTs were identified that encode polypeptides resembling phytocyanins, plant-specific proteins constituting a distinct family of mononuclear blue copper proteins. One of them encodes plantacyanin from Arubidopsis. while three others, designated as uclacyanin 1, 2, and 3, encode protein precursors that are closely related to precursors of stellacyanins and a blue copper protein from pea pods. Comparative analyses with known phytocyanins allow further classification of these proteins into three distinct subfamilies designated as uclacyanins, stellacyanins, and plantacyanins. This specification is based on (1) their spectroscopic properties, (2) their glycosylation state, (3) the domain organization of their precursors, and (4) their copper-binding amino acids. The recombinant copper binding domain of Arubidopsis uclacyanin I was expressed, purified, and shown to bind a copper atom in a fashion known as "blue" or type 1. The mutant of cucumber stellacyanin in which the glutamine axial ligand was substituted by a methionine (Q99M) was purified and shown to possess spectroscopic properties similar to uclacyanin I rather than to plantacyanins. Its redox potential was determined by cyclic voltammetry to be +420 mV, a value that is significantly higher than that determined for the wild-type protein (+260 mV). The available structural data suggest that stellacyanins (and possibly other phytocyanins) might not be diffusible electron-transfer proteins participating in long-range electron-transfer processes. Conceivably, they are involved in redox reactions occurring during primary defense responses in plants and/or in lignin formation.

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“…MCOs use a minimum of four Cu centers: a ''blue,'' type 1 Cu site and a trinuclear Cu cluster composed of a ''normal,'' type 2 Cu and a binuclear type 3 Cu site that together catalyze the 4-electron reduction of O 2 to water with concomitant oxidation of substrates (2,3). Crystal structures indicate that both the type 3 Cu active sites in Hc/CatO/Tyr (4-10) and the MCOs (11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25) are similarly held in the protein by three His ligands on each Cu center. No additional ligands are present in the deoxy forms, whereas oxygen-derived ligands bridge and exchange couple the two Cu(II)s in the oxidized forms.…”

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confidence: 99%

Geometric and electronic structure differences between the type 3 copper sites of the multicopper oxidases and hemocyanin/tyrosinase

Yoon

Fujii

Solomon

2009

Proc. Natl. Acad. Sci. U.S.A.

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The X-ray structure of human serum ceruloplasmin at 3.1 Å: nature of the copper centres

Cited by 364 publications

References 0 publications

Aceruloplasminemia with Juvenile-onset Diabetes Mellitus Caused by Exon Skipping in the Ceruloplasmin Gene

Aceruloplasminemia with Juvenile-onset Diabetes Mellitus Caused by Exon Skipping in the Ceruloplasmin Gene

Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of phytocyanins: Plant‐specific mononuclear blue copper proteins

Geometric and electronic structure differences between the type 3 copper sites of the multicopper oxidases and hemocyanin/tyrosinase

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