6r8n: Difference between revisions

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New page: '''Unreleased structure''' The entry 6r8n is ON HOLD Authors: Colletier, J.-P., Gauto, D., Estrozi, L., Favier, A., Effantin, G., Schoehn, G., Boisbouvier, J., Schanda, P. Description:...
 
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'''Unreleased structure'''


The entry 6r8n is ON HOLD
==STRUCTURE DETERMINATION OF THE TETRAHEDRAL AMINOPEPTIDASE TET2 FROM P. HORIKOSHII BY USE OF COMBINED SOLID-STATE NMR, SOLUTION-STATE NMR AND EM DATA 4.1 A, FOLLOWED BY REAL_SPACE_REFINEMENT AT 4.1 A==
<SX load='6r8n' size='340' side='right' viewer='molstar' caption='[[6r8n]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6r8n]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R8N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R8N FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy , Hybrid , Solution NMR, [[Resolution|Resolution]] 4.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6r8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r8n OCA], [https://pdbe.org/6r8n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r8n RCSB], [https://www.ebi.ac.uk/pdbsum/6r8n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r8n ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TET_PYRHO TET_PYRHO] Functions as an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. However, can also cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. Has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity. Is involved in protein degradation, performing degradation of oligopeptides produced by the proteasome into single amino acids.<ref>PMID:15375159</ref> <ref>PMID:15713475</ref> <ref>PMID:15736957</ref>


Authors: Colletier, J.-P., Gauto, D., Estrozi, L., Favier, A., Effantin, G., Schoehn, G., Boisbouvier, J., Schanda, P.
==See Also==
 
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
Description: STRUCTURE DETERMINATION OF THE TETRAHEDRAL AMINOPEPTIDASE TET2 FROM P. HORIKOSHII BY USE OF COMBINED SOLID-STATE NMR, SOLUTION-STATE NMR AND EM DATA 4.1 A, FOLLOWED BY REAL_SPACE_REFINEMENT AT 4.1 A
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Boisbouvier, J]]
__TOC__
[[Category: Schoehn, G]]
</SX>
[[Category: Effantin, G]]
[[Category: Large Structures]]
[[Category: Colletier, J.-P]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Estrozi, L]]
[[Category: Boisbouvier J]]
[[Category: Schanda, P]]
[[Category: Colletier J-P]]
[[Category: Gauto, D]]
[[Category: Effantin G]]
[[Category: Favier, A]]
[[Category: Estrozi L]]
[[Category: Favier A]]
[[Category: Gauto D]]
[[Category: Schanda P]]
[[Category: Schoehn G]]
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