2nye
From Proteopedia
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==Overview== | ==Overview== | ||
| - | AMP-activated protein kinase (AMPK) is a central regulator of energy | + | AMP-activated protein kinase (AMPK) is a central regulator of energy homeostasis in mammals. AMP is believed to control the activity of AMPK by binding to the gamma subunit of this heterotrimeric enzyme. This subunit contains two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. No structural information is currently available on this subunit, and the molecular basis for its interactions with AMP is not well understood. We report here the crystal structure at 1.9 Angstrom resolution of the Bateman2 domain of Snf4, the gamma subunit of the yeast ortholog of AMPK. The structure revealed a dimer of the Bateman2 domain, and this dimerization is supported by our light-scattering, mutagenesis, and biochemical studies. There is a prominent pocket at the center of this dimer, and most of the disease-causing mutations are located in or near this pocket. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Amodeo, G | + | [[Category: Amodeo, G A.]] |
[[Category: Carlson, M.]] | [[Category: Carlson, M.]] | ||
[[Category: Hong, S.]] | [[Category: Hong, S.]] | ||
[[Category: Iram, S.]] | [[Category: Iram, S.]] | ||
[[Category: Pirino, G.]] | [[Category: Pirino, G.]] | ||
| - | [[Category: Rudolph, M | + | [[Category: Rudolph, M J.]] |
[[Category: Tong, L.]] | [[Category: Tong, L.]] | ||
[[Category: amp kinase]] | [[Category: amp kinase]] | ||
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[[Category: snf4]] | [[Category: snf4]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:12:27 2008'' |
Revision as of 16:12, 21 February 2008
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Crystal structure of the Bateman2 domain of yeast Snf4
Overview
AMP-activated protein kinase (AMPK) is a central regulator of energy homeostasis in mammals. AMP is believed to control the activity of AMPK by binding to the gamma subunit of this heterotrimeric enzyme. This subunit contains two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. No structural information is currently available on this subunit, and the molecular basis for its interactions with AMP is not well understood. We report here the crystal structure at 1.9 Angstrom resolution of the Bateman2 domain of Snf4, the gamma subunit of the yeast ortholog of AMPK. The structure revealed a dimer of the Bateman2 domain, and this dimerization is supported by our light-scattering, mutagenesis, and biochemical studies. There is a prominent pocket at the center of this dimer, and most of the disease-causing mutations are located in or near this pocket.
About this Structure
2NYE is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure of the Bateman2 domain of yeast Snf4: dimeric association and relevance for AMP binding., Rudolph MJ, Amodeo GA, Iram SH, Hong SP, Pirino G, Carlson M, Tong L, Structure. 2007 Jan;15(1):65-74. PMID:17223533
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