2ibp
From Proteopedia
(New page: 200px<br /><applet load="2ibp" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ibp, resolution 1.60Å" /> '''Crystal Structure of...) |
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==Overview== | ==Overview== | ||
| - | A growing number of organisms have been discovered inhabiting extreme | + | A growing number of organisms have been discovered inhabiting extreme environments, including temperatures in excess of 100 degrees C. How cellular proteins from such organisms retain their native folds under extreme conditions is still not fully understood. Recent computational and structural studies have identified disulfide bonding as an important mechanism for stabilizing intracellular proteins in certain thermophilic microbes. Here, we present the first proteomic analysis of intracellular disulfide bonding in the hyperthermophilic archaeon Pyrobaculum aerophilum. Our study reveals that the utilization of disulfide bonds extends beyond individual proteins to include many protein-protein complexes. We report the 1.6 A crystal structure of one such complex, a citrate synthase homodimer. The structure contains two intramolecular disulfide bonds, one per subunit, which result in the cyclization of each protein chain in such a way that the two chains are topologically interlinked, rendering them inseparable. This unusual feature emphasizes the variety and sophistication of the molecular mechanisms that can be achieved by evolution. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Pyrobaculum aerophilum]] | [[Category: Pyrobaculum aerophilum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Boutz, D | + | [[Category: Boutz, D R.]] |
[[Category: Cascio, D.]] | [[Category: Cascio, D.]] | ||
| - | [[Category: Yeates, T | + | [[Category: Yeates, T O.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: thermophilic]] | [[Category: thermophilic]] | ||
| - | ''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 17:51:08 2008'' |
Revision as of 15:51, 21 February 2008
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Crystal Structure of Citrate Synthase from Pyrobaculum aerophilum
Overview
A growing number of organisms have been discovered inhabiting extreme environments, including temperatures in excess of 100 degrees C. How cellular proteins from such organisms retain their native folds under extreme conditions is still not fully understood. Recent computational and structural studies have identified disulfide bonding as an important mechanism for stabilizing intracellular proteins in certain thermophilic microbes. Here, we present the first proteomic analysis of intracellular disulfide bonding in the hyperthermophilic archaeon Pyrobaculum aerophilum. Our study reveals that the utilization of disulfide bonds extends beyond individual proteins to include many protein-protein complexes. We report the 1.6 A crystal structure of one such complex, a citrate synthase homodimer. The structure contains two intramolecular disulfide bonds, one per subunit, which result in the cyclization of each protein chain in such a way that the two chains are topologically interlinked, rendering them inseparable. This unusual feature emphasizes the variety and sophistication of the molecular mechanisms that can be achieved by evolution.
About this Structure
2IBP is a Single protein structure of sequence from Pyrobaculum aerophilum with and as ligands. Active as Citrate (Si)-synthase, with EC number 2.3.3.1 Full crystallographic information is available from OCA.
Reference
Discovery of a thermophilic protein complex stabilized by topologically interlinked chains., Boutz DR, Cascio D, Whitelegge J, Perry LJ, Yeates TO, J Mol Biol. 2007 May 18;368(5):1332-44. Epub 2007 Mar 6. PMID:17395198
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