4JDE

Crystal structure of PUD-1/PUD-2 heterodimer

Summary for 4JDE

• Entry DOI: 10.2210/pdb4jde/pdb
• Descriptor: Protein F15E11.13, Protein F15E11.1, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: beta sandwich, unknown function
• Biological source: Caenorhabditis elegans (nematode); More
• Total number of polymer chains: 2
• Total formula weight: 33525.41

Authors

Luo, S.,Ye, K. (deposition date: 2013-02-25, release date: 2013-11-06, Last modification date: 2024-03-20)

Primary citation

Ding, Y.H.,Du, Y.G.,Luo, S.,Li, Y.X.,Li, T.M.,Yoshina, S.,Wang, X.,Klage, K.,Mitani, S.,Ye, K.,Dong, M.Q.
Characterization of PUD-1 and PUD-2, two proteins up-regulated in a long-lived daf-2 mutant.
Plos One, 8:e67158-e67158, 2013

PubMed Abstract: C. elegans PUD-1 and PUD-2, two proteins up-regulated in daf-2(loss-of-function) (PUD), are homologous 17-kD proteins with a large abundance increase in long-lived daf-2 mutant animals of reduced insulin signaling. In this study, we show that both PUD-1 and PUD-2 are abundantly expressed in the intestine and hypodermis, and form a heterodimer. We have solved their crystal structure to 1.9-Å resolution and found that both proteins adopt similar β-sandwich folds in the V-shaped dimer. In contrast, their homologs PUD-3, PUD-4, PUDL-1 and PUDL-2 are all monomeric proteins with distinct expression patterns in C. elegans. Thus, the PUD-1/PUD-2 heterodimer probably has a function distinct from their family members. Neither overexpression nor deletion of pud-1 and pud-2 affected the lifespan of WT or daf-2 mutant animals, suggesting that their induction in daf-2 worms does not contribute to longevity. Curiously, deletion of pud-1 and pud-2 was associated with a protective effect against paralysis induced by the amyloid β-peptide (1-42), which further enhanced the protection conferred by daf-2(RNAi) against Aβ.

PubMed: 23799143
DOI: 10.1371/journal.pone.0067158

Experimental method

X-RAY DIFFRACTION (1.9 Å)