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3w09

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Current revision (12:44, 8 November 2023) (edit) (undo)
 
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<StructureSection load='3w09' size='340' side='right'caption='[[3w09]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3w09' size='340' side='right'caption='[[3w09]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3w09]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W09 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3w09]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/tern/Australia/G70C/1975(H11N9)) Influenza A virus (A/tern/Australia/G70C/1975(H11N9))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W09 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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZGE:(2R,3R,4R)-3-ACETAMIDO-4-CARBAMIMIDAMIDO-5-FLUORANYL-2-[(1R,2R)-1,2,3-TRIS(OXIDANYL)PROPYL]-3,4-DIHYDRO-2H-PYRAN-6-CARBOXYLIC+ACID'>ZGE</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1nnc|1nnc]], [[7nn9|7nn9]]</div></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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZGE:(2R,3R,4R)-3-ACETAMIDO-4-CARBAMIMIDAMIDO-5-FLUORANYL-2-[(1R,2R)-1,2,3-TRIS(OXIDANYL)PROPYL]-3,4-DIHYDRO-2H-PYRAN-6-CARBOXYLIC+ACID'>ZGE</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/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </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=3w09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w09 OCA], [https://pdbe.org/3w09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w09 RCSB], [https://www.ebi.ac.uk/pdbsum/3w09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w09 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=3w09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w09 OCA], [https://pdbe.org/3w09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w09 RCSB], [https://www.ebi.ac.uk/pdbsum/3w09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w09 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/NRAM_I75A5 NRAM_I75A5]] Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.
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[https://www.uniprot.org/uniprot/NRAM_I75A5 NRAM_I75A5] Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Exo-alpha-sialidase]]
 
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[[Category: Influenza a virus]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Streltsov, V A]]
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[[Category: Streltsov VA]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Neuraminidase]]
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[[Category: Sialidase]]
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Current revision

Influenza virus neuraminidase subtype N9 (TERN) complexed with 2,3-dif guanidino-neu5ac2en inhibitor

PDB ID 3w09

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