3C2H

Crystal Structure of SYS-1 at 2.6A resolution

Summary for 3C2H

• Entry DOI: 10.2210/pdb3c2h/pdb
• Related: 3C2G
• Descriptor: Sys-1 protein, CITRATE ANION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: sys-1, caenorhabditis elegans, beta-catenin, wnt, cell adhesion
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 2
• Total formula weight: 142424.15

Authors

Liu, J.,Phillips, B.T.,Amaya, M.F.,Kimble, J.,Xu, W. (deposition date: 2008-01-25, release date: 2008-05-20, Last modification date: 2024-02-21)

Primary citation

Liu, J.,Phillips, B.T.,Amaya, M.F.,Kimble, J.,Xu, W.
The C. elegans SYS-1 protein is a bona fide beta-catenin.
Dev.Cell, 14:751-761, 2008

PubMed Abstract: C. elegans SYS-1 has key functional characteristics of a canonical beta-catenin, but no significant sequence similarity. Here, we report the SYS-1 crystal structure, both on its own and in a complex with POP-1, the C. elegans TCF homolog. The two structures possess signature features of canonical beta-catenin and the beta-catenin/TCF complex that could not be predicted by sequence. Most importantly, SYS-1 bears 12 armadillo repeats and the SYS-1/POP-1 interface is anchored by a conserved salt-bridge, the "charged button." We also modeled structures for three other C. elegans beta-catenins to predict the molecular basis of their distinct binding properties. Finally, we generated a phylogenetic tree, using the region of highest structural similarity between SYS-1 and beta-catenin, and found that SYS-1 clusters robustly within the beta-catenin clade. We conclude that the SYS-1 protein belongs to the beta-catenin family and suggest that additional divergent beta-catenins await discovery.

PubMed: 18477457
DOI: 10.1016/j.devcel.2008.02.015

Experimental method

X-RAY DIFFRACTION (2.6 Å)