1rki
From Proteopedia
(New page: 200px<br /><applet load="1rki" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rki, resolution 1.60Å" /> '''Structure of pag5_73...) |
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| - | [[Image:1rki.gif|left|200px]]<br /><applet load="1rki" size=" | + | [[Image:1rki.gif|left|200px]]<br /><applet load="1rki" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rki, resolution 1.60Å" /> | caption="1rki, resolution 1.60Å" /> | ||
'''Structure of pag5_736 from P. aerophilum with three disulphide bonds'''<br /> | '''Structure of pag5_736 from P. aerophilum with three disulphide bonds'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Thermophilic organisms flourish in varied high-temperature environmental | + | Thermophilic organisms flourish in varied high-temperature environmental niches that are deadly to other organisms. Recently, genomic evidence has implicated a critical role for disulfide bonds in the structural stabilization of intracellular proteins from certain of these organisms, contrary to the conventional view that structural disulfide bonds are exclusively extracellular. Here both computational and structural data are presented to explore the occurrence of disulfide bonds as a protein-stabilization method across many thermophilic prokaryotes. Based on computational studies, disulfide-bond richness is found to be widespread, with thermophiles containing the highest levels. Interestingly, only a distinct subset of thermophiles exhibit this property. A computational search for proteins matching this target phylogenetic profile singles out a specific protein, known as protein disulfide oxidoreductase, as a potential key player in thermophilic intracellular disulfide-bond formation. Finally, biochemical support in the form of a new crystal structure of a thermophilic protein with three disulfide bonds is presented together with a survey of known structures from the literature. Together, the results provide insight into biochemical specialization and the diversity of methods employed by organisms to stabilize their proteins in exotic environments. The findings also motivate continued efforts to sequence genomes from divergent organisms. |
==About this Structure== | ==About this Structure== | ||
| - | 1RKI 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 ACT, SO4, CL, P6G and PG4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1RKI 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>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=P6G:'>P6G</scene> and <scene name='pdbligand=PG4:'>PG4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RKI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Beeby, M.]] | [[Category: Beeby, M.]] | ||
| - | [[Category: Boutz, D | + | [[Category: Boutz, D R.]] |
| - | [[Category: Perry, L | + | [[Category: Perry, L J.]] |
[[Category: Ryttersgaard, C.]] | [[Category: Ryttersgaard, C.]] | ||
| - | [[Category: Yeates, T | + | [[Category: Yeates, T O.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:53 2008'' |
Revision as of 12:51, 21 February 2008
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Structure of pag5_736 from P. aerophilum with three disulphide bonds
Overview
Thermophilic organisms flourish in varied high-temperature environmental niches that are deadly to other organisms. Recently, genomic evidence has implicated a critical role for disulfide bonds in the structural stabilization of intracellular proteins from certain of these organisms, contrary to the conventional view that structural disulfide bonds are exclusively extracellular. Here both computational and structural data are presented to explore the occurrence of disulfide bonds as a protein-stabilization method across many thermophilic prokaryotes. Based on computational studies, disulfide-bond richness is found to be widespread, with thermophiles containing the highest levels. Interestingly, only a distinct subset of thermophiles exhibit this property. A computational search for proteins matching this target phylogenetic profile singles out a specific protein, known as protein disulfide oxidoreductase, as a potential key player in thermophilic intracellular disulfide-bond formation. Finally, biochemical support in the form of a new crystal structure of a thermophilic protein with three disulfide bonds is presented together with a survey of known structures from the literature. Together, the results provide insight into biochemical specialization and the diversity of methods employed by organisms to stabilize their proteins in exotic environments. The findings also motivate continued efforts to sequence genomes from divergent organisms.
About this Structure
1RKI is a Single protein structure of sequence from Pyrobaculum aerophilum with , , , and as ligands. Full crystallographic information is available from OCA.
Reference
The genomics of disulfide bonding and protein stabilization in thermophiles., Beeby M, O'Connor BD, Ryttersgaard C, Boutz DR, Perry LJ, Yeates TO, PLoS Biol. 2005 Sep;3(9):e309. Epub 2005 Aug 23. PMID:16111437
Page seeded by OCA on Thu Feb 21 14:51:53 2008
Categories: Pyrobaculum aerophilum | Single protein | Beeby, M. | Boutz, D R. | Perry, L J. | Ryttersgaard, C. | Yeates, T O. | ACT | CL | P6G | PG4 | SO4 | (beta-alpha-beta)x2 | Beta-loop-beta-beta | Cxxc motif | Structural genomics
