6lz1
From Proteopedia
(Difference between revisions)
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==Structure of S.pombe alpha-mannosidase Ams1== | ==Structure of S.pombe alpha-mannosidase Ams1== | ||
| - | <StructureSection load='6lz1' size='340' side='right'caption='[[6lz1]]' scene=''> | + | <StructureSection load='6lz1' size='340' side='right'caption='[[6lz1]], [[Resolution|resolution]] 3.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>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 [http://proteopedia.org/fgij/fg.htm?mol=6LZ1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6lz1]] is a 4 chain structure with sequence from [http://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 [http://proteopedia.org/fgij/fg.htm?mol=6LZ1 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6lz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lz1 OCA], [http://pdbe.org/6lz1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lz1 RCSB], [http://www.ebi.ac.uk/pdbsum/6lz1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lz1 ProSAT]</span></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ams1, mns2, SPAC513.05 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6lz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lz1 OCA], [http://pdbe.org/6lz1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lz1 RCSB], [http://www.ebi.ac.uk/pdbsum/6lz1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lz1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MAN1_SCHPO MAN1_SCHPO]] Degrades free oligosaccharides in the vacuole. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| + | |||
| + | 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> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6lz1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Alpha-mannosidase]] | ||
| + | [[Category: Fission yeast]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Ye K]] | + | [[Category: Ye, K]] |
| - | [[Category: Zhang J]] | + | [[Category: Zhang, J]] |
| + | [[Category: Glycoside hydrolase]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 20:42, 28 October 2020
Structure of S.pombe alpha-mannosidase Ams1
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