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==Combined solid-state NMR, solution-state NMR and EM data for structure determination of the tetrahedral aminopeptidase TET2 from P. horikoshii==
==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=''>
<SX load='6f3k' size='340' side='right' viewer='molstar' caption='[[6f3k]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6f3k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. 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>
<table><tr><td colspan='2'>[[6f3k]] is a 1 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=6F3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F3K FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy , Hybrid , Solid-state NMR , Solution NMR, [[Resolution|Resolution]] 4.1&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">frvX, PH1527 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70601 Pyrococcus horikoshii])</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'>[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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6f3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f3k OCA], [https://pdbe.org/6f3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f3k RCSB], [https://www.ebi.ac.uk/pdbsum/6f3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f3k ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[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==
==See Also==
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<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pyrococcus horikoshii]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Boisbouvier, J]]
[[Category: Boisbouvier J]]
[[Category: Colletier, J P]]
[[Category: Colletier JP]]
[[Category: Effantin, G]]
[[Category: Effantin G]]
[[Category: Estrozi, L F]]
[[Category: Estrozi LF]]
[[Category: Favier, A]]
[[Category: Favier A]]
[[Category: Gauto, D F]]
[[Category: Gauto DF]]
[[Category: Kerfah, R]]
[[Category: Kerfah R]]
[[Category: Macek, P]]
[[Category: Macek P]]
[[Category: Schanda, P]]
[[Category: Schanda P]]
[[Category: Schoehn, G]]
[[Category: Schoehn G]]
[[Category: Schwieters, C D]]
[[Category: Schwieters CD]]
[[Category: Sivertsen, A C]]
[[Category: Sivertsen AC]]
[[Category: Sounier, R]]
[[Category: Sounier R]]
[[Category: Aminopeptidase]]
[[Category: Oligomer]]
[[Category: Peptidase]]
[[Category: Peptide binding protein]]
[[Category: Protein quality control]]

Latest revision as of 19:02, 14 March 2024

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

6f3k, resolution 4.10Å

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