6f3k: Difference between revisions

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'''Unreleased structure'''


The entry 6f3k is ON HOLD
==Combined solid-state NMR, solution-state NMR and EM data for structure determination of the tetrahedral aminopeptidase TET2 from P. horikoshii==
 
<StructureSection load='6f3k' size='340' side='right' caption='[[6f3k]], [[Resolution|resolution]] 4.10&Aring;, [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
Authors: Gauto, D.F., Estrozi, L.F., Schwieters, C.D., Effantin, G., Macek, P., Sounier, R., Kerfah, R., Sivertsen, A.C., Colletier, J.P., Boisbouvier, J., Schoehn, G., Favier, A., Schanda, P.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6f3k]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F3K FirstGlance]. <br>
Description: Combined solid-state NMR, solution-state NMR and EM data for structure determination of the tetrahedral aminopeptidase TET2 from P. horikoshii
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6f3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f3k OCA], [http://pdbe.org/6f3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f3k RCSB], [http://www.ebi.ac.uk/pdbsum/6f3k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f3k ProSAT]</span></td></tr>
[[Category: Schoehn, G]]
</table>
== Function ==
[[http://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> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Boisbouvier, J]]
[[Category: Boisbouvier, J]]
[[Category: Gauto, D.F]]
[[Category: Colletier, J P]]
[[Category: Colletier, J.P]]
[[Category: Sounier, R]]
[[Category: Sivertsen, A.C]]
[[Category: Effantin, G]]
[[Category: Effantin, G]]
[[Category: Estrozi, L F]]
[[Category: Favier, A]]
[[Category: Gauto, D F]]
[[Category: Kerfah, R]]
[[Category: Macek, P]]
[[Category: Macek, P]]
[[Category: Kerfah, R]]
[[Category: Schanda, P]]
[[Category: Schanda, P]]
[[Category: Estrozi, L.F]]
[[Category: Schoehn, G]]
[[Category: Schwieters, C.D]]
[[Category: Schwieters, C D]]
[[Category: Favier, A]]
[[Category: Sivertsen, A C]]
[[Category: Sounier, R]]
[[Category: Aminopeptidase]]
[[Category: Oligomer]]
[[Category: Peptidase]]
[[Category: Peptide binding protein]]
[[Category: Protein quality control]]

Revision as of 09:33, 14 March 2018

Combined solid-state NMR, solution-state NMR and EM data for structure determination of the tetrahedral aminopeptidase TET2 from P. horikoshiiCombined solid-state NMR, solution-state NMR and EM data for structure determination of the tetrahedral aminopeptidase TET2 from P. horikoshii

Structural highlights

6f3k is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.[1] [2] [3]

References

  1. ↑ Russo S, Baumann U. Crystal structure of a dodecameric tetrahedral-shaped aminopeptidase. J Biol Chem. 2004 Dec 3;279(49):51275-81. Epub 2004 Sep 16. PMID:15375159 doi:10.1074/jbc.M409455200
  2. ↑ Borissenko L, Groll M. Crystal structure of TET protease reveals complementary protein degradation pathways in prokaryotes. J Mol Biol. 2005 Mar 11;346(5):1207-19. Epub 2005 Jan 16. PMID:15713475 doi:10.1016/j.jmb.2004.12.056
  3. ↑ Dura MA, Receveur-Brechot V, Andrieu JP, Ebel C, Schoehn G, Roussel A, Franzetti B. Characterization of a TET-like aminopeptidase complex from the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemistry. 2005 Mar 8;44(9):3477-86. PMID:15736957 doi:http://dx.doi.org/10.1021/bi047736j
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