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3C2G

Crystal complex of SYS-1/POP-1 at 2.5A resolution

Summary for 3C2G
Entry DOI10.2210/pdb3c2g/pdb
Related3C2H
DescriptorSys-1 protein, Pop-1 8-residue peptide (3 entities in total)
Functional Keywordsbeta-catenin, phylogeny, sys-1, pop-1, caenorhabditis elegans, developmental protein, dna-binding, nucleus, cell adhesion-transcription complex, cell adhesion/transcription
Biological sourceCaenorhabditis elegans
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Cellular locationNucleus : Q10666
Total number of polymer chains4
Total formula weight145175.69
Authors
Liu, J.,Phillips, B.T.,Amaya, M.F.,Kimble, J.,Xu, W. (deposition date: 2008-01-24, release date: 2008-05-20, Last modification date: 2024-10-30)
Primary citationLiu, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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