4r8f: Difference between revisions

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==Crystal structure of yeast aminopeptidase 1 (Ape1)==
==Crystal structure of yeast aminopeptidase 1 (Ape1)==
<StructureSection load='4r8f' size='340' side='right' caption='[[4r8f]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='4r8f' size='340' side='right'caption='[[4r8f]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4r8f]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8F FirstGlance]. <br>
<table><tr><td colspan='2'>[[4r8f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8F FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminopeptidase_I Aminopeptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.22 3.4.11.22] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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=4r8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8f RCSB], [http://www.ebi.ac.uk/pdbsum/4r8f PDBsum]</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=4r8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8f OCA], [https://pdbe.org/4r8f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8f RCSB], [https://www.ebi.ac.uk/pdbsum/4r8f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8f ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/AMPL_YEAST AMPL_YEAST]] Resident vacuolar enzyme that catalyzes the removal of amino acids from the N-terminus of peptides and proteins. Also acts as the major cargo protein of the cytoplasm-to-vacuole targeting (Cvt) pathway. The precursor form of aminopeptidase 1 (prApe1) assembles into dodecamers and the propeptide mediates the aggregation of dodecamers into higher multimers. The multimers are then recognized via the propeptide by their receptor ATG19, and ATG19 further interacts with ATG11, which tethers the APE1-ATG19 complex to the pre-autophagosomal structure (PAS). The cargo-receptor complex (also Cvt complex) is selectively enwrapped by a double-membrane structure termed the Cvt vesicle under vegetative growth conditions and by a similar but larger double-membrane structure termed the autophagosome under nitrogen starvation conditions. The Cvt vesicle or the autophagosome fuses with the vacuolar membrane and release its content in the vacuolar lumen. In the vacuole, prApe1 is processed into mature aminopeptidase 1 (mApe1).<ref>PMID:11382752</ref> <ref>PMID:11430817</ref> <ref>PMID:15138258</ref> <ref>PMID:22123825</ref> <ref>PMID:363165</ref> <ref>PMID:8901576</ref> <ref>PMID:9214379</ref> <ref>PMID:9412464</ref>
[https://www.uniprot.org/uniprot/AMPL_YEAST AMPL_YEAST] Resident vacuolar enzyme that catalyzes the removal of amino acids from the N-terminus of peptides and proteins. Also acts as the major cargo protein of the cytoplasm-to-vacuole targeting (Cvt) pathway. The precursor form of aminopeptidase 1 (prApe1) assembles into dodecamers and the propeptide mediates the aggregation of dodecamers into higher multimers. The multimers are then recognized via the propeptide by their receptor ATG19, and ATG19 further interacts with ATG11, which tethers the APE1-ATG19 complex to the pre-autophagosomal structure (PAS). The cargo-receptor complex (also Cvt complex) is selectively enwrapped by a double-membrane structure termed the Cvt vesicle under vegetative growth conditions and by a similar but larger double-membrane structure termed the autophagosome under nitrogen starvation conditions. The Cvt vesicle or the autophagosome fuses with the vacuolar membrane and release its content in the vacuolar lumen. In the vacuole, prApe1 is processed into mature aminopeptidase 1 (mApe1).<ref>PMID:11382752</ref> <ref>PMID:11430817</ref> <ref>PMID:15138258</ref> <ref>PMID:22123825</ref> <ref>PMID:363165</ref> <ref>PMID:8901576</ref> <ref>PMID:9214379</ref> <ref>PMID:9412464</ref>  
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4r8f" style="background-color:#fffaf0;"></div>
==See Also==
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aminopeptidase I]]
[[Category: Large Structures]]
[[Category: Chang, C I]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Su, M Y]]
[[Category: Chang C-I]]
[[Category: Autophagy]]
[[Category: Su M-Y]]
[[Category: Cvt pathway]]
[[Category: Hydrolase]]
[[Category: Peptidase]]

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