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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 DOI10.2210/pdb2pmi/pdb
Related2PK9
DescriptorCyclin-dependent protein kinase PHO85, PHO85 cyclin PHO80, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (4 entities in total)
Functional Keywordscyclin-dependent kinase, cyclin, signaling protein, transferase-cell cycle complex, transferase/cell cycle
Biological sourceSaccharomyces cerevisiae (baker's yeast)
More
Cellular locationCytoplasm: P17157 P20052
Total number of polymer chains4
Total formula weight140174.63
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 citationHuang, 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: 18042456
DOI: 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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건을2025-02-05부터공개중

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