2NPM

crystal structure of Cryptosporidium parvum 14-3-3 protein in complex with peptide

Summary for 2NPM

• Entry DOI: 10.2210/pdb2npm/pdb
• Descriptor: 14-3-3 domain containing protein, CONSENSUS PEPTIDE FOR 14-3-3 PROTEINS (3 entities in total)
• Functional Keywords: cell regulator protein 14-3-3, cryptosporidium parvum, structural genomics, structural genomics consortium, sgc, protein binding
• Biological source: Cryptosporidium parvum
• Total number of polymer chains: 4
• Total formula weight: 61016.74

Authors

Dong, A.,Lew, J.,Wasney, G.,Ren, H.,Lin, L.,Hassanali, A.,Qiu, W.,Zhao, Y.,Doyle, D.,Vedadi, M.,Koeieradzki, I.,Edwards, A.M.,Arrowsmith, C.H.,Weigelt, J.,Sundstrom, M.,Bochkarev, A.,Hui, R.,Brokx, S.,Structural Genomics Consortium (SGC) (deposition date: 2006-10-27, release date: 2006-11-07, Last modification date: 2024-11-20)

Primary citation

Brokx, S.J.,Wernimont, A.K.,Dong, A.,Wasney, G.A.,Lin, Y.H.,Lew, J.,Vedadi, M.,Lee, W.H.,Hui, R.
Characterization of 14-3-3 proteins from Cryptosporidium parvum.
Plos One, 6:e14827-e14827, 2011

PubMed Abstract: The parasite Cryptosporidium parvum has three 14-3-3 proteins: Cp14ε, Cp14a and Cp14b, with only Cp14ε similar to human 14-3-3 proteins in sequence, peptide-binding properties and structure. Structurally, Cp14a features the classical 14-3-3 dimer but with a uniquely wide pocket and a disoriented RRY triad potentially incapable of binding phosphopeptides. The Cp14b protein deviates from the norm significantly: (i) In one subunit, the phosphorylated C-terminal tail is bound in the binding groove like a phosphopeptide. This supports our binding study indicating this protein was stabilized by a peptide mimicking its last six residues. (ii) The other subunit has eight helices instead of nine, with αA and αB forming a single helix and occluding the peptide-binding cleft. (iii) The protein forms a degenerate dimer with the two binding grooves divided and facing opposite directions. These features conspire to block and disrupt the bicameral substrate-binding pocket, suggesting a possible tripartite auto-regulation mechanism that has not been observed previously.

PubMed: 21853016
DOI: 10.1371/journal.pone.0014827

Experimental method

X-RAY DIFFRACTION (2.52 Å)