1rki
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1rki.gif|left|200px]] | [[Image:1rki.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1rki", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | | | + | {{STRUCTURE_1rki| PDB=1rki | SCENE= }} |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''Structure of pag5_736 from P. aerophilum with three disulphide bonds''' | '''Structure of pag5_736 from P. aerophilum with three disulphide bonds''' | ||
| Line 30: | Line 27: | ||
[[Category: Ryttersgaard, C.]] | [[Category: Ryttersgaard, C.]] | ||
[[Category: Yeates, T O.]] | [[Category: Yeates, T O.]] | ||
| - | [[Category: | + | [[Category: Beta-loop-beta-beta]] |
| - | + | [[Category: Cxxc motif]] | |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:36:34 2008'' |
| - | + | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 04:36, 3 May 2008
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. 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 Sat May 3 07:36:34 2008
