2PMI
Structure of the Pho85-Pho80 CDK-cyclin Complex of the Phosphate-responsive Signal Transduction Pathway with Bound ATP-gamma-S
Summary for 2PMI
Entry DOI | 10.2210/pdb2pmi/pdb |
Related | 2PK9 |
Descriptor | Cyclin-dependent protein kinase PHO85, PHO85 cyclin PHO80, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (4 entities in total) |
Functional Keywords | cyclin-dependent kinase, cyclin, signaling protein, transferase-cell cycle complex, transferase/cell cycle |
Biological source | Saccharomyces cerevisiae (baker's yeast) More |
Cellular location | Cytoplasm: P17157 P20052 |
Total number of polymer chains | 4 |
Total formula weight | 140174.63 |
Authors | Huang, K.,Ferrin-O'Connell, I.,Zhang, W.,Leonard, G.A.,O'Shea, E.K.,Quiocho, F.A. (deposition date: 2007-04-23, release date: 2007-12-11, Last modification date: 2023-08-30) |
Primary citation | Huang, K.,Ferrin-O'Connell, I.,Zhang, W.,Leonard, G.A.,O'Shea, E.K.,Quiocho, F.A. Structure of the Pho85-Pho80 CDK-Cyclin Complex of the Phosphate-Responsive Signal Transduction Pathway Mol.Cell, 28:614-623, 2007 Cited by PubMed Abstract: The ability to sense and respond appropriately to environmental changes is a primary requirement of all living organisms. In response to phosphate limitation, Saccharomyces cerevisiae induces transcription of a set of genes involved in the regulation of phosphate acquisition from the ambient environment. A signal transduction pathway (the PHO pathway) mediates this response, with Pho85-Pho80 playing a vital role. Here we report the X-ray structure of Pho85-Pho80, a prototypic structure of a CDK-cyclin complex functioning in transcriptional regulation in response to environmental changes. The structure revealed a specific salt link between a Pho85 arginine and a Pho80 aspartate that makes phosphorylation of the Pho85 activation loop dispensable and that maintains a Pho80 loop conformation for possible substrate recognition. It further showed two sites on the Pho80 cyclin for high-affinity binding of the transcription factor substrate (Pho4) and the CDK inhibitor (Pho81) that are markedly distant to each other and the active site. PubMed: 18042456DOI: 10.1016/j.molcel.2007.09.013 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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