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6r8n
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==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]] 4.10Å' 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]] 4.1Å</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> | ||
| - | + | ==See Also== | |
| - | + | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </SX> |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Pyrococcus horikoshii OT3]] |
| - | [[Category: Estrozi | + | [[Category: Boisbouvier J]] |
| - | [[Category: | + | [[Category: Colletier J-P]] |
| - | [[Category: Gauto | + | [[Category: Effantin G]] |
| - | [[Category: | + | [[Category: Estrozi L]] |
| + | [[Category: Favier A]] | ||
| + | [[Category: Gauto D]] | ||
| + | [[Category: Schanda P]] | ||
| + | [[Category: Schoehn G]] | ||
Current revision
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
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