2cf4: Difference between revisions
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<StructureSection load='2cf4' size='340' side='right'caption='[[2cf4]], [[Resolution|resolution]] 3.08Å' scene=''> | <StructureSection load='2cf4' size='340' side='right'caption='[[2cf4]], [[Resolution|resolution]] 3.08Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2cf4]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2cf4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CF4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cf4 OCA], [https://pdbe.org/2cf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cf4 RCSB], [https://www.ebi.ac.uk/pdbsum/2cf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cf4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 10:31, 2 February 2022
Pyrococcus horikoshii TET1 peptidase can assemble into a tetrahedron or a large octahedral shellPyrococcus horikoshii TET1 peptidase can assemble into a tetrahedron or a large octahedral shell
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCellular proteolysis involves large oligomeric peptidases that play key roles in the regulation of many cellular processes. The cobalt-activated peptidase TET1 from the hyperthermophilic Archaea Pyrococcus horikoshii (PhTET1) was found to assemble as a 12-subunit tetrahedron and as a 24-subunit octahedral particle. Both quaternary structures were solved by combining x-ray crystallography and cryoelectron microscopy data. The internal organization of the PhTET1 particles reveals highly self-compartmentalized systems made of networks of access channels extended by vast catalytic chambers. The two edifices display aminopeptidase activity, and their organizations indicate substrate navigation mechanisms different from those described in other large peptidase complexes. Compared with the tetrahedron, the octahedron forms a more expanded hollow structure, representing a new type of giant peptidase complex. PhTET1 assembles into two different quaternary structures because of quasi-equivalent contacts that previously have only been identified in viral capsids. An archaeal peptidase assembles into two different quaternary structures: A tetrahedron and a giant octahedron.,Schoehn G, Vellieux FM, Asuncion Dura M, Receveur-Brechot V, Fabry CM, Ruigrok RW, Ebel C, Roussel A, Franzetti B J Biol Chem. 2006 Nov 24;281(47):36327-37. Epub 2006 Sep 14. PMID:16973604[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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