2rih
From Proteopedia
(New page: '''Unreleased structure''' The entry 2rih is ON HOLD until Paper Publication Authors: Lee, T.M., King, N.P., Sawaya, M.R., Cascio, D., Yeates, T.O. Description: CBS domain protein PAE2...) |
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| - | + | [[Image:2rih.jpg|left|200px]] | |
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| + | {{STRUCTURE_2rih| PDB=2rih | SCENE= }} | ||
| - | + | '''CBS domain protein PAE2072 from Pyrobaculum aerophilum''' | |
| - | Description: CBS domain protein PAE2072 from Pyrobaculum aerophilum | ||
| + | ==Overview== | ||
| + | Cystathionine beta-synthase domains are found in a myriad of proteins from organisms across the tree of life and have been hypothesized to function as regulatory modules that sense the energy charge of cells. Here we characterize the structure and stability of PAE2072, a dimeric tandem cystathionine beta-synthase domain protein from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. Crystal structures of the protein in unliganded and AMP-bound forms, determined at resolutions of 2.10 and 2.35 A, respectively, reveal remarkable conservation of key functional features seen in the gamma subunit of the eukaryotic AMP-activated protein kinase. The structures also confirm the presence of a suspected intermolecular disulfide bond between the two subunits that is shown to stabilize the protein. Our AMP-bound structure represents a first step in investigating the function of a large class of uncharacterized prokaryotic proteins. In addition, this work extends previous studies that have suggested that, in certain thermophilic microbes, disulfide bonds play a key role in stabilizing intracellular proteins and protein-protein complexes. | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun | + | ==About this Structure== |
| + | 2RIH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RIH OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | Structures and functional implications of an AMP-binding cystathionine beta-synthase domain protein from a hyperthermophilic archaeon., King NP, Lee TM, Sawaya MR, Cascio D, Yeates TO, J Mol Biol. 2008 Jun 27;380(1):181-92. Epub 2008 May 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18513746 18513746] | ||
| + | [[Category: Pyrobaculum aerophilum]] | ||
| + | [[Category: Single protein]] | ||
| + | [[Category: Cascio, D.]] | ||
| + | [[Category: King, N P.]] | ||
| + | [[Category: Lee, T M.]] | ||
| + | [[Category: Sawaya, M R.]] | ||
| + | [[Category: Yeates, T O.]] | ||
| + | [[Category: Amp binding protein]] | ||
| + | [[Category: Bateman domain]] | ||
| + | [[Category: Cbs domain]] | ||
| + | [[Category: Ligand-binding protein]] | ||
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:04:18 2008'' | ||
Revision as of 09:04, 18 June 2008
CBS domain protein PAE2072 from Pyrobaculum aerophilum
Overview
Cystathionine beta-synthase domains are found in a myriad of proteins from organisms across the tree of life and have been hypothesized to function as regulatory modules that sense the energy charge of cells. Here we characterize the structure and stability of PAE2072, a dimeric tandem cystathionine beta-synthase domain protein from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. Crystal structures of the protein in unliganded and AMP-bound forms, determined at resolutions of 2.10 and 2.35 A, respectively, reveal remarkable conservation of key functional features seen in the gamma subunit of the eukaryotic AMP-activated protein kinase. The structures also confirm the presence of a suspected intermolecular disulfide bond between the two subunits that is shown to stabilize the protein. Our AMP-bound structure represents a first step in investigating the function of a large class of uncharacterized prokaryotic proteins. In addition, this work extends previous studies that have suggested that, in certain thermophilic microbes, disulfide bonds play a key role in stabilizing intracellular proteins and protein-protein complexes.
About this Structure
2RIH is a Single protein structure of sequence from Pyrobaculum aerophilum. Full crystallographic information is available from OCA.
Reference
Structures and functional implications of an AMP-binding cystathionine beta-synthase domain protein from a hyperthermophilic archaeon., King NP, Lee TM, Sawaya MR, Cascio D, Yeates TO, J Mol Biol. 2008 Jun 27;380(1):181-92. Epub 2008 May 7. PMID:18513746 Page seeded by OCA on Wed Jun 18 12:04:18 2008
