6lz1

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Current revision (10:47, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6lz1' size='340' side='right'caption='[[6lz1]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='6lz1' size='340' side='right'caption='[[6lz1]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6lz1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LZ1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6lz1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LZ1 FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ams1, mns2, SPAC513.05 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</td></tr>
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<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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6lz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lz1 OCA], [https://pdbe.org/6lz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lz1 RCSB], [https://www.ebi.ac.uk/pdbsum/6lz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lz1 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=6lz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lz1 OCA], [https://pdbe.org/6lz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lz1 RCSB], [https://www.ebi.ac.uk/pdbsum/6lz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lz1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/MAN1_SCHPO MAN1_SCHPO]] Degrades free oligosaccharides in the vacuole.
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[https://www.uniprot.org/uniprot/MAN1_SCHPO MAN1_SCHPO] Degrades free oligosaccharides in the vacuole.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Fungal alpha-mannosidase Ams1 and its mammalian homolog MAN2C1 hydrolyze terminal alpha-linked mannoses in free oligosaccharides released from misfolded glycoproteins or lipid-linked oligosaccharide donors. Ams1 is transported by selective autophagy into vacuoles. Here, we determine the tetrameric structure of Ams1 from the fission yeast Schizosaccharomyces pombe at 3.2 A resolution by cryo-electron microscopy. Distinct from a low resolution structure of S. cerevisiae Ams1, S. pombe Ams1 has a prominent N-terminal tail that mediates tetramerization and an extra beta-sheet domain. Ams1 shares a conserved active site with other enzymes in glycoside hydrolase family 38, to which Ams1 belongs, but contains extra N-terminal domains involved in tetramerization. The atomic structure of Ams1 reported here will aid understanding of its enzymatic activity and transport mechanism.
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Cryo-EM structure of fission yeast tetrameric alpha-mannosidase Ams1.,Zhang J, Wang YY, Du LL, Ye K FEBS Open Bio. 2020 Sep 27. doi: 10.1002/2211-5463.12988. PMID:32981237<ref>PMID:32981237</ref>
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==See Also==
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*[[Mannosidase 3D structures|Mannosidase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6lz1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Alpha-mannosidase]]
 
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[[Category: Fission yeast]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ye, K]]
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[[Category: Schizosaccharomyces pombe 972h-]]
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[[Category: Zhang, J]]
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[[Category: Ye K]]
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[[Category: Glycoside hydrolase]]
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[[Category: Zhang J]]
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[[Category: Hydrolase]]
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Current revision

Structure of S.pombe alpha-mannosidase Ams1

PDB ID 6lz1

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