Structure of a CutA1 divalent-cation tolerance protein from Cryptosporidium parvum, the protozoal parasite responsible for cryptosporidiosis

Journal Article · Fri May 01 00:00:00 EDT 2015 · Acta Crystallographica. Section F, Structural Biology Communications

DOI:https://doi.org/10.1107/S2053230X14028210· OSTI ID:1193227

Buchko, Garry W. ^[1]; Robinson, Howard ^[2]; Abendroth, Jan ^[3]; Clitfon, Mathew C. ^[4]; Zhang, Yanfeng ^[5]; Hewitt, Stephen N. ^[6]; Staker, Bart L. ^[7]; Van Voorhis, Wesley C. ^[6]; Mylera, Peter J. ^[8]

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1. Seattle Structural Genomics Center for Infectious Diesease, Seattle, WA (United States); Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
2. Brookhaven National Lab. (BNL), Upton, NY (United States)
3. Seattle Structural Genomics Center for Infectious Diesease, Seattle, WA (United States); Beryllium, Bainbridge Island, WA (United States)
4. Seattle Structural Genomics Center for Infectious Diesease, Seattle, WA (United States);Beryllium, Bainbridge Island, WA (United States)
5. Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
6. Seattle Structural Genomics Center for Infectious Diesease, Seattle, WA (United States); Univ. of Washington, Seattle, WA (United States)
7. Seattle Structural Genomics Center for Infectious Diesease, Seattle, WA (United States); Seattle Biomedical Research Institute, Seattle, WA (United States)
8. Seattle Structural Genomics Center for Infectious Diesease, Seattle, WA (United States); Seattle Biomedical Research Institute, Seattle, WA (United States); Univ. of Washington, Seattle, WA (United States)

Cryptosporidiosis is an infectious disease caused by protozoan parasites from the Cryptosporidium species. Infection is associated with mild to severe diarrhea that usually resolves spontaneously in healthy human adults, but may lead to severe complications in young children and in immunocompromised patients. The genome of Cryptosporidium parvum contains a gene, CUTA_CRYPI, that may play a role in regulating the intracellular concentration of copper, a toxic element if left unchecked. Here we report the crystal structure for this CutA1 protein, Cp-CutA1, is reported at 2.0 Å resolution (4E98). As observed for other CutA1 structures, the 117-residue protein is a trimer with a core ferrodoxin-like fold. Circular dichroism spectroscopy shows little unfolding of Cp-CutA1 up to 353 K. This robustness is corroborated by ¹H-¹⁵N HSQC spectra at 333 K that is characteristic of a folded protein, suggesting NMR spectroscopy may be a useful tool to further probe the function of the CutA1 proteins. While robust, Cp-CutA1 is not as stable as the homologous protein from a hyperthermophile, perhaps due to a wide β-bulgein β2 that protrudes P48 and S49 outside the β-sheet.

• Research Organization: Brookhaven National Laboratory (BNL), Upton, NY (United States)
• Sponsoring Organization: USDOE Office of Science (SC)
• Grant/Contract Number: SC00112704
• OSTI ID: 1193227
• Report Number(s): BNL-108113-2015-JA; ACSFEN; R&D Project: LS001
• Journal Information: Acta Crystallographica. Section F, Structural Biology Communications, Vol. 71, Issue 5; ISSN 2053-230X
• Publisher: International Union of Crystallography
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
Cryptosporidium parvum
divalent-cation tolerance protein
CutA1
cryptosporidiosis