1Q1O
Solution Structure of the PB1 Domain of Cdc24p (Long Form)
Summary for 1Q1O
| Entry DOI | 10.2210/pdb1q1o/pdb |
| Related | 1IP9 1IPG |
| NMR Information | BMRB: 5875 |
| Descriptor | Cell division control protein 24 (1 entity in total) |
| Functional Keywords | pb1 domain, pccr, pc motif, opca motif, yeast, cell polarity, protein-protein interaction, signaling protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 11211.43 |
| Authors | Yoshinaga, S.,Kohjima, M.,Ogura, K.,Yokochi, M.,Takeya, R.,Ito, T.,Sumimoto, H.,Inagaki, F. (deposition date: 2003-07-22, release date: 2003-10-14, Last modification date: 2024-05-29) |
| Primary citation | Yoshinaga, S.,Kohjima, M.,Ogura, K.,Yokochi, M.,Takeya, R.,Ito, T.,Sumimoto, H.,Inagaki, F. The PB1 domain and the PC motif-containing region are structurally similar protein binding modules EMBO J., 22:4888-4897, 2003 Cited by PubMed Abstract: The PC motif is evolutionarily conserved together with the PB1 domain, a binding partner of the PC motif-containing protein. For interaction with the PB1 domain, the PC motif-containing region (PCCR) comprising the PC motif and its flanking regions is required. Because the PB1 domain and the PCCR are novel binding modules found in a variety of signaling proteins, their structural and functional characterization is crucial. Bem1p and Cdc24p interact through the PB1-PCCR interaction and regulate cell polarization in budding yeast. Here, we determined a tertiary structure of the PCCR of Cdc24p by NMR. The tertiary structure of the PCCR is similar to that of the PB1 domain of Bem1p, which is classified into a ubiquitin fold. The PC motif portion takes a compact betabetaalpha-fold, presented on the ubiquitin scaffold. Mutational studies indicate that the PB1-PCCR interaction is mainly electrostatic. Based on the structural information, we group the PB1 domains and the PCCRs into a novel family, named the PB1 family. Thus, the PB1 family proteins form a specific dimer with each other. PubMed: 14517229DOI: 10.1093/emboj/cdg475 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
