2l4f

NMR structure of the UBA domain of S. cerevisiae Dcn1 bound to ubiquitinNMR structure of the UBA domain of S. cerevisiae Dcn1 bound to ubiquitin

Structural highlights

2l4f is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DCN1_YEAST Required for neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity. Does not act by preventing deneddylation, but rather facilitates neddylation, possibly by acting with HRT1/RBX1 to recruit the Nedd8-charged E2 UBC12 to the cullin component of SCF-type complexes.^[1]

References

↑ Kurz T, Ozlu N, Rudolf F, O'Rourke SM, Luke B, Hofmann K, Hyman AA, Bowerman B, Peter M. The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae. Nature. 2005 Jun 30;435(7046):1257-61. PMID:15988528 doi:http://dx.doi.org/nature03662

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OCA

[1] Kurz T, Ozlu N, Rudolf F, O'Rourke SM, Luke B, Hofmann K, Hyman AA, Bowerman B, Peter M. The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae. Nature. 2005 Jun 30;435(7046):1257-61. PMID:15988528 doi:http://dx.doi.org/nature03662

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