4E98
Crystal structure of possible CutA1 divalent ion tolerance protein from Cryptosporidium parvum Iowa II
Summary for 4E98
| Entry DOI | 10.2210/pdb4e98/pdb |
| Descriptor | CutA1 divalent ion tolerance protein, CHLORIDE ION (3 entities in total) |
| Functional Keywords | ssgcid, structural genomics, seattle structural genomics center for infectious disease, signaling protein |
| Biological source | Cryptosporidium parvum |
| Total number of polymer chains | 3 |
| Total formula weight | 46863.42 |
| Authors | Seattle Structural Genomics Center for Infectious Disease (SSGCID),Buchko, G.W.,Robinson, H. (deposition date: 2012-03-20, release date: 2012-04-11, Last modification date: 2023-09-13) |
| Primary citation | Buchko, G.W.,Abendroth, J.,Clifton, M.C.,Robinson, H.,Zhang, Y.,Hewitt, S.N.,Staker, B.L.,Edwards, T.E.,Van Voorhis, W.C.,Myler, P.J. Structure of a CutA1 divalent-cation tolerance protein from Cryptosporidium parvum, the protozoal parasite responsible for cryptosporidiosis. Acta Crystallogr F Struct Biol Commun, 71:522-530, 2015 Cited by PubMed Abstract: Cryptosporidiosis is an infectious disease caused by protozoan parasites of the Cryptosporidium genus. 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 C. parvum contains a gene, CUTA_CRYPI, that may play a role in regulating the intracellular concentration of copper, which is a toxic element in excess. Here, the crystal structure of this CutA1 protein, Cp-CutA1, is reported at 2.0 Å resolution. As observed for other CutA1 structures, the 117-residue protein is a trimer with a core ferrodoxin-like fold. Circular dichroism spectroscopy shows little, in any, unfolding of Cp-CutA1 up to 353 K. This robustness is corroborated by (1)H-(15)N HSQC spectra at 333 K, which are characteristic of a folded protein, suggesting that 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 owing to a wide β-bulge in β2 that protrudes Pro48 and Ser49 outside the β-sheet. PubMed: 25945704DOI: 10.1107/S2053230X14028210 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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