1pqs
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Solution structure of the C-terminal OPCA domain of yCdc24p
OverviewOverview
Phox 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.
About this StructureAbout this Structure
1PQS is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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
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