1wmi
From Proteopedia
(New page: 200px<br /><applet load="1wmi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wmi, resolution 2.3Å" /> '''Crystal structure of ...) |
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| - | [[Image:1wmi.gif|left|200px]]<br /><applet load="1wmi" size=" | + | [[Image:1wmi.gif|left|200px]]<br /><applet load="1wmi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wmi, resolution 2.3Å" /> | caption="1wmi, resolution 2.3Å" /> | ||
'''Crystal structure of archaeal RelE-RelB complex from Pyrococcus horikoshii OT3'''<br /> | '''Crystal structure of archaeal RelE-RelB complex from Pyrococcus horikoshii OT3'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Escherichia coli chromosome encodes toxin-antitoxin pairs. The toxin | + | The Escherichia coli chromosome encodes toxin-antitoxin pairs. The toxin RelE cleaves mRNA positioned at the A-site in ribosomes, whereas the antitoxin RelB relieves the effect of RelE. The hyperthermophilic archaeon Pyrococcus horikoshii OT3 has the archaeal homologs aRelE and aRelB. Here we report the crystal structure of aRelE in complex with aRelB determined at a resolution of 2.3 A. aRelE folds into an alpha/beta structure, whereas aRelB lacks a distinct hydrophobic core and extensively wraps around the molecular surface of aRelE. Neither component shows structural homology to known ribonucleases or their inhibitors. Site-directed mutagenesis suggests that Arg85, in the C-terminal region, is strongly involved in the functional activity of aRelE, whereas Arg40, Leu48, Arg58 and Arg65 play a modest role in the toxin's activity. |
==About this Structure== | ==About this Structure== | ||
| - | 1WMI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii_ot3 Pyrococcus horikoshii ot3]. Full crystallographic information is available from [http:// | + | 1WMI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii_ot3 Pyrococcus horikoshii ot3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WMI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: toxin-antitoxin complex]] | [[Category: toxin-antitoxin complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:45:56 2008'' |
Revision as of 13:45, 21 February 2008
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Crystal structure of archaeal RelE-RelB complex from Pyrococcus horikoshii OT3
Overview
The Escherichia coli chromosome encodes toxin-antitoxin pairs. The toxin RelE cleaves mRNA positioned at the A-site in ribosomes, whereas the antitoxin RelB relieves the effect of RelE. The hyperthermophilic archaeon Pyrococcus horikoshii OT3 has the archaeal homologs aRelE and aRelB. Here we report the crystal structure of aRelE in complex with aRelB determined at a resolution of 2.3 A. aRelE folds into an alpha/beta structure, whereas aRelB lacks a distinct hydrophobic core and extensively wraps around the molecular surface of aRelE. Neither component shows structural homology to known ribonucleases or their inhibitors. Site-directed mutagenesis suggests that Arg85, in the C-terminal region, is strongly involved in the functional activity of aRelE, whereas Arg40, Leu48, Arg58 and Arg65 play a modest role in the toxin's activity.
About this Structure
1WMI is a Protein complex structure of sequences from Pyrococcus horikoshii ot3. Full crystallographic information is available from OCA.
Reference
Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects., Takagi H, Kakuta Y, Okada T, Yao M, Tanaka I, Kimura M, Nat Struct Mol Biol. 2005 Apr;12(4):327-31. Epub 2005 Mar 13. PMID:15768033
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