4E98

Crystal structure of possible CutA1 divalent ion tolerance protein from Cryptosporidium parvum Iowa II

4E98 の概要

• エントリーDOI: 10.2210/pdb4e98/pdb
• 分子名称: CutA1 divalent ion tolerance protein, CHLORIDE ION (3 entities in total)
• 機能のキーワード: ssgcid, structural genomics, seattle structural genomics center for infectious disease, signaling protein
• 由来する生物種: Cryptosporidium parvum
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 46863.42

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID),Buchko, G.W.,Robinson, H. (登録日: 2012-03-20, 公開日: 2012-04-11, 最終更新日: 2023-09-13)

主引用文献

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

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: 25945704
DOI: 10.1107/S2053230X14028210

実験手法

X-RAY DIFFRACTION (2 Å)