1PQS

Solution structure of the C-terminal OPCA domain of yCdc24p

Summary for 1PQS

• Entry DOI: 10.2210/pdb1pqs/pdb
• Descriptor: Cell division control protein 24 (1 entity in total)
• Functional Keywords: alpha and beta protein, cell cycle
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 8973.03

Authors

Leitner, D.,Wahl, M.,Labudde, D.,Diehl, A.,Schmieder, P.,Pires, J.R.,Fossi, M.,Leidert, M.,Krause, G.,Oschkinat, H. (deposition date: 2003-06-19, release date: 2003-07-01, Last modification date: 2024-05-29)

Primary citation

Leitner, D.,Wahl, M.,Labudde, D.,Krause, G.,Diehl, A.,Schmieder, P.,Pires, J.R.,Fossi, M.,Wiedemann, U.,Leidert, M.,Oschkinat, H.
The solution structure of an N-terminally truncated version of the yeast CDC24p PB1 domain shows a different beta-sheet topology.
Febs Lett., 579:3534-3538, 2005

PubMed Abstract: 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.

PubMed: 15961083
DOI: 10.1016/j.febslet.2005.05.025

Experimental method

SOLUTION NMR