The solution structure of an N-terminally truncated version of the yeast CDC24p PB1 domain shows a different beta-sheet topology
| Autor: | Dietmar Leitner, Peter Schmieder, Anne Diehl, Dirk Labudde, Martin Wahl, José R. Pires, Michele Fossi, Martina Leidert, Urs Wiedemann, Gerd Krause, Hartmut Oschkinat |
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| Rok vydání: | 2005 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Saccharomyces cerevisiae Molecular Sequence Data Biophysics Beta sheet Cell Cycle Proteins Nuclear Overhauser effect Bud emergence MSB1 interacting 1 Topology Biochemistry Protein Structure Secondary Structural Biology Genetics Guanine Nucleotide Exchange Factors Amino Acid Sequence Molecular Biology Phox and Bem1 family Sequence Deletion Budding biology Chemistry virus diseases Cell Biology Cell cycle biochemical phenomena metabolism and nutrition Cell division cycle 24 biology.organism_classification Yeast Protein Structure Tertiary Solutions OPR/PC/AID motif Nuclear magnetic resonance structure Two-dimensional nuclear magnetic resonance spectroscopy Heteronuclear single quantum coherence spectroscopy |
| Zdroj: | FEBS letters. 579(17) |
| ISSN: | 0014-5793 |
| Popis: | Phox and Bem1 (PB1) domains mediate protein-pro- tein 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) dur- ing 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 b-sheet than the long form. However, the C-terminal part of the structure shows the con- served PB1 domain features including the OPCA motif with a slight rearrangement of helix a1. Residues which are important for the heterodimerization with BEM1p are structurally pre- served. � 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies. |
| Databáze: | OpenAIRE |
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