Structural Interplay between Calcium(<scp>II</scp>) and Copper(<scp>II</scp>) Binding to S100A13 Protein

Arnesano, Fabio; Banci, Lucia; Bertini, Ivano; Fantoni, Adele; Tenori, Leonardo; Viezzoli, Maria Silvia

doi:10.1002/anie.200500540

Cited by 46 publications

(39 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The structural consequences of Cu 2+ binding to S100A13 have been investigated using solution NMR (Arnesano et al, 2005). Comparisons between apo, Ca 2+ -loaded and Ca 2+ , Cu 2+ -loaded S100A13 revealed Cu 2+ causes an additional, minor opening of the Helix III-IV interface relative to the Ca 2+ -loaded state.…”

Section: Binding Of Coppermentioning

confidence: 99%

“…These correlated with electron paramagnetic resonance (EPR) studies that assigned the Cu 2+ coordination as pseudo-tetragonal with nitrogen and oxygen donor atoms. An unexpected aspect of their analysis was that the Cu 2+ ions are completely exposed to solvent, unlike the typical transition metal sites that are buried within the S100 proteins (Arnesano et al, 2005). The authors suggested that exposure of the metal may help regulate the interaction of S100A13 with target proteins, but no data was provided in support of this speculation.…”

Section: Binding Of Coppermentioning

confidence: 99%

See 1 more Smart Citation

Binding of transition metals to S100 proteins

Gilston

Skaar

Chazin

2016

Sci. China Life Sci.

View full text Add to dashboard Cite

The S100 proteins are a unique class of EF-hand Ca2+ binding proteins distributed in a cell-specific, tissue-specific, and cell cycle-specific manner in humans and other vertebrates. These proteins are distinguished by their distinctive homodimeric structure, both intracellular and extracellular functions, and the ability to bind transition metals at the dimer interface. Here we summarize current knowledge of S100 protein binding of Zn2+, Cu2+ and Mn2+ ions, focusing on binding affinities, conformational changes that arise from metal binding, and the roles of transition metal binding in S100 protein function.

show abstract

Section: Binding Of Coppermentioning

confidence: 99%

Section: Binding Of Coppermentioning

confidence: 99%

Binding of transition metals to S100 proteins

Gilston

Skaar

Chazin

2016

Sci. China Life Sci.

View full text Add to dashboard Cite

show abstract

“…As mentioned above, Cu is another important micronutrient for microbes, particularly eukaryotic microbes (2). To date, CP binding to Cu has not been reported, although fluorescence studies suggest that Cu can induce conformational changes in CP (36), and other S100 proteins, including S100B, S100A12, and S100A13, have been shown to bind this metal ion (37)(38)(39)(40), raising the possibility of a role for CP in Cu sequestration.…”

mentioning

confidence: 99%

Role of Calprotectin in Withholding Zinc and Copper from Candida albicans

et al. 2018

View full text Add to dashboard Cite

The opportunistic fungal pathogen Candida albicans acquires essential metals from the host, yet the host can sequester these micronutrients through a process known as nutritional immunity. How the host withholds metals from C. albicans has been poorly understood; here we examine the role of calprotectin (CP), a transition metal binding protein. When CP depletes bioavailable Zn from the extracellular environment, C. albicans strongly upregulates ZRT1 and PRA1 for Zn import and maintains constant intracellular Zn through numerous cell divisions. We show for the first time that CP can also sequester Cu by binding Cu(II) with subpicomolar affinity. CP blocks fungal acquisition of Cu from serum and induces a Cu starvation stress response involving SOD1 and SOD3 superoxide dismutases. These transcriptional changes are mirrored when C. albicans invades kidneys in a mouse model of disseminated candidiasis, although the responses to Cu and Zn limitations are temporally distinct. The Cu response progresses throughout 72 h, while the Zn response is short-lived. Notably, these stress responses were attenuated in CP null mice, but only at initial stages of infection. Thus, Zn and Cu pools are dynamic at the hostpathogen interface and CP acts early in infection to restrict metal nutrients from C. albicans.

show abstract

“…Human S100A13 consists of 98 amino-acid residues and has a molecular weight of 11 kDa. The solution structures of the apo-and Ca 2+ -bound forms of human S100A13 at pH 5.6 (PDB codes 1yus and 1yuu, respectively; Arnesano et al, 2005) have previously been reported. Here, we report the crystallization of Ca 2+ -bound human S100A13 at physiological pH (pH 7.5).…”

Section: +mentioning

confidence: 99%

“…The interaction of S100A13 with these proteins depends on the presence of Cu 2+ ions . The Cu 2+ -binding sites of S100A13 are likely to be formed by Ca 2+ binding (Arnesano et al, 2005), which is mediated by Ca 2+ influx through N-type Ca…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary X-ray analysis of human S100A13

et al. 2006

View full text Add to dashboard Cite

S100A13 is a member of the S100 family of EF-hand-containing calcium-binding proteins and plays an important role in the secretion of fibroblast growth factor-1 and interleukin 1, two pro-angiogenic factors released by the endoplasmic reticulum/Golgi-independent non-classical secretory pathway. Human S100A13 was heterologously expressed in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion method using PEG 3350 as the precipitant. The crystals diffracted X-rays from a synchrotron-radiation source to 1.8 Å resolution and the space group was assigned as primitive orthorhombic P2 1 2 1 2 1 .

show abstract

Structural Interplay between Calcium(II) and Copper(II) Binding to S100A13 Protein

Cited by 46 publications

References 18 publications

Binding of transition metals to S100 proteins

Binding of transition metals to S100 proteins

Role of Calprotectin in Withholding Zinc and Copper from Candida albicans

Crystallization and preliminary X-ray analysis of human S100A13

Contact Info

Product

Resources

About