1y0r: Difference between revisions

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[[Image:1y0r.png|left|200px]]


{{STRUCTURE_1y0r|  PDB=1y0r  |  SCENE=  }}
==Crystal structure of the tetrahedral aminopeptidase from P. horikoshii==
 
<StructureSection load='1y0r' size='340' side='right'caption='[[1y0r]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
===Crystal structure of the tetrahedral aminopeptidase from P. horikoshii===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1y0r]] 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=1Y0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y0R FirstGlance]. <br>
{{ABSTRACT_PUBMED_15713475}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARS:ARSENIC'>ARS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y0r OCA], [https://pdbe.org/1y0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y0r RCSB], [https://www.ebi.ac.uk/pdbsum/1y0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y0r ProSAT]</span></td></tr>
[[1y0r]] is a 1 chain structure of [[Aminopeptidase]] 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=1Y0R OCA].  
</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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y0/1y0r_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=1y0r ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Aminopeptidase|Aminopeptidase]]
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:015713475</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus horikoshii]]
[[Category: Pyrococcus horikoshii]]
[[Category: Borissenko, L.]]
[[Category: Borissenko L]]
[[Category: Groll, M.]]
[[Category: Groll M]]
[[Category: Aminopeptidase domain]]
[[Category: Hydrolase]]
[[Category: Pdz domain]]

Latest revision as of 16:37, 13 March 2024

Crystal structure of the tetrahedral aminopeptidase from P. horikoshiiCrystal structure of the tetrahedral aminopeptidase from P. horikoshii

Structural highlights

1y0r is a 1 chain structure with sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
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]

Evolutionary Conservation

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

See Also

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

1y0r, resolution 1.75Å

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