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| {{STRUCTURE_2ibp| PDB=2ibp | SCENE= }} | | {{STRUCTURE_2ibp| PDB=2ibp | SCENE= }} |
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| '''Crystal Structure of Citrate Synthase from Pyrobaculum aerophilum'''
| | ===Crystal Structure of Citrate Synthase from Pyrobaculum aerophilum=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17395198}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17395198 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17395198}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Homodimer]] | | [[Category: Homodimer]] |
| [[Category: Thermophilic]] | | [[Category: Thermophilic]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:18:18 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:14:31 2008'' |
