2wyr
From Proteopedia
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| - | [[ | + | ==3-D STRUCTURE OF PHTET1-12S, DODECAMER IN THE ASYMMETRIC UNIT== |
| + | <StructureSection load='2wyr' size='340' side='right' caption='[[2wyr]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2wyr]] is a 12 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=2WYR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WYR FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cf4|2cf4]]</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=2wyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wyr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wyr RCSB], [http://www.ebi.ac.uk/pdbsum/2wyr PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cellular 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<ref>PMID:16973604</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Aminopeptidase|Aminopeptidase]] | *[[Aminopeptidase|Aminopeptidase]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Pyrococcus horikoshii]] | [[Category: Pyrococcus horikoshii]] | ||
[[Category: Dura, M A.]] | [[Category: Dura, M A.]] | ||
Revision as of 00:57, 2 October 2014
3-D STRUCTURE OF PHTET1-12S, DODECAMER IN THE ASYMMETRIC UNIT
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