1wmi: Difference between revisions

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==Crystal structure of archaeal RelE-RelB complex from Pyrococcus horikoshii OT3==
==Crystal structure of archaeal RelE-RelB complex from Pyrococcus horikoshii OT3==
<StructureSection load='1wmi' size='340' side='right' caption='[[1wmi]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1wmi' size='340' side='right'caption='[[1wmi]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1wmi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WMI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WMI FirstGlance]. <br>
<table><tr><td colspan='2'>[[1wmi]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WMI FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wmi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wmi RCSB], [http://www.ebi.ac.uk/pdbsum/1wmi PDBsum]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<table>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wmi OCA], [https://pdbe.org/1wmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wmi RCSB], [https://www.ebi.ac.uk/pdbsum/1wmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wmi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O73966_PYRHO O73966_PYRHO]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wm/1wmi_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wm/1wmi_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wmi ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:15768033</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Pyrococcus horikoshii]]
[[Category: Large Structures]]
[[Category: Kakuta, Y.]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Kamachi, R.]]
[[Category: Kakuta Y]]
[[Category: Kimura, M.]]
[[Category: Kamachi R]]
[[Category: Takagi, H.]]
[[Category: Kimura M]]
[[Category: Tanaka, I.]]
[[Category: Takagi H]]
[[Category: Yao, M.]]
[[Category: Tanaka I]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Yao M]]
[[Category: Toxin-antitoxin complex]]

Latest revision as of 16:32, 13 March 2024

Crystal structure of archaeal RelE-RelB complex from Pyrococcus horikoshii OT3Crystal structure of archaeal RelE-RelB complex from Pyrococcus horikoshii OT3

Structural highlights

1wmi is a 4 chain structure with sequence from Pyrococcus horikoshii OT3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

O73966_PYRHO

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1wmi, resolution 2.30Å

Drag the structure with the mouse to rotate

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OCA