2ibp

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[[Image:2ibp.jpg|left|200px]]<br /><applet load="2ibp" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ibp.jpg|left|200px]]
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caption="2ibp, resolution 1.60&Aring;" />
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'''Crystal Structure of Citrate Synthase from Pyrobaculum aerophilum'''<br />
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{{Structure
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|PDB= 2ibp |SIZE=350|CAPTION= <scene name='initialview01'>2ibp</scene>, resolution 1.60&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Citrate_(Si)-synthase Citrate (Si)-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.1 2.3.3.1]
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|GENE= PAE1689 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13773 Pyrobaculum aerophilum])
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}}
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'''Crystal Structure of Citrate Synthase from Pyrobaculum aerophilum'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2IBP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Citrate_(Si)-synthase Citrate (Si)-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.1 2.3.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IBP OCA].
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2IBP 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=2IBP OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17395198 17395198]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17395198 17395198]
[[Category: Citrate (Si)-synthase]]
[[Category: Citrate (Si)-synthase]]
[[Category: Pyrobaculum aerophilum]]
[[Category: Pyrobaculum aerophilum]]
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[[Category: thermophilic]]
[[Category: thermophilic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:51:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:27:36 2008''

Revision as of 15:27, 20 March 2008


PDB ID 2ibp

Drag the structure with the mouse to rotate
, resolution 1.60Å
Ligands: and
Gene: PAE1689 (Pyrobaculum aerophilum)
Activity: Citrate (Si)-synthase, with EC number 2.3.3.1
Coordinates: save as pdb, mmCIF, xml



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. 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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