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Solution structure of the C-terminal OPCA domain of yCdc24pSolution structure of the C-terminal OPCA domain of yCdc24p
Structural highlights
FunctionCDC24_YEAST Promotes the exchange of CDC42-bound GDP by GTP. Controls the polarity of calmodulin, and the calcium regulatory process of bud emergence. CDC24 may be involved in the initial selection and organization of the budding site. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPhox and Bem1 (PB1) domains mediate protein-protein interactions via the formation of homo- or hetero-dimers. The C-terminal PB1 domain of yeast cell division cycle 24 (CDC24p), a guanine-nucleotide exchange factor involved in cell polarity establishment, is known to interact with the PB1 domain occurring in bud emergence MSB1 interacting 1 (BEM1p) during the regulation of the yeast budding process via its OPR/PC/AID (OPCA) motif. Here, we present the structure of an N-terminally truncated version of the Sc CDC24p PB1 domain. It shows a different topology of the beta-sheet than the long form. However, the C-terminal part of the structure shows the conserved PB1 domain features including the OPCA motif with a slight rearrangement of helix alpha1. Residues which are important for the heterodimerization with BEM1p are structurally preserved. The solution structure of an N-terminally truncated version of the yeast CDC24p PB1 domain shows a different beta-sheet topology.,Leitner D, Wahl M, Labudde D, Krause G, Diehl A, Schmieder P, Pires JR, Fossi M, Wiedemann U, Leidert M, Oschkinat H FEBS Lett. 2005 Jul 4;579(17):3534-8. PMID:15961083[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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