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2pmi

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(New page: 200px<br /><applet load="2pmi" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pmi, resolution 2.90&Aring;" /> '''Structure of the Pho...)
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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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Structure of the Pho85-Pho80 CDK-Cyclin Complex of the Phosphate-Responsive Signal Transduction Pathway., Huang K, Ferrin-O'Connell I, Zhang W, Leonard GA, O'Shea EK, Quiocho FA, Mol Cell. 2007 Nov 30;28(4):614-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18042456 18042456]
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Structure of the Pho85-Pho80 CDK-cyclin complex of the phosphate-responsive signal transduction pathway., Huang K, Ferrin-O'Connell I, Zhang W, Leonard GA, O'Shea EK, Quiocho FA, Mol Cell. 2007 Nov 30;28(4):614-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18042456 18042456]
[[Category: Cyclin-dependent kinase]]
[[Category: Cyclin-dependent kinase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Connell, I.Ferrin-O.]]
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[[Category: Connell, I Ferrin-O.]]
[[Category: Huang, K.]]
[[Category: Huang, K.]]
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[[Category: Leonard, G.A.]]
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[[Category: Leonard, G A.]]
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[[Category: Quiocho, F.A.]]
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[[Category: Quiocho, F A.]]
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[[Category: Shea, E.K.O.]]
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[[Category: Shea, E K.O.]]
[[Category: Zhang, W.]]
[[Category: Zhang, W.]]
[[Category: MES]]
[[Category: MES]]
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[[Category: transferase/cell cycle complex]]
[[Category: transferase/cell cycle complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:43:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:31:00 2008''

Revision as of 16:31, 21 February 2008


2pmi, resolution 2.90Å

Drag the structure with the mouse to rotate

Structure of the Pho85-Pho80 CDK-cyclin Complex of the Phosphate-responsive Signal Transduction Pathway with Bound ATP-gamma-S

Overview

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.

About this Structure

2PMI is a Protein complex structure of sequences from Saccharomyces cerevisiae with and as ligands. Active as Cyclin-dependent kinase, with EC number 2.7.11.22 Full crystallographic information is available from OCA.

Reference

Structure of the Pho85-Pho80 CDK-cyclin complex of the phosphate-responsive signal transduction pathway., Huang K, Ferrin-O'Connell I, Zhang W, Leonard GA, O'Shea EK, Quiocho FA, Mol Cell. 2007 Nov 30;28(4):614-23. PMID:18042456

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