5huk: Difference between revisions

No edit summary
No edit summary
 
Line 1: Line 1:


==The crystal structure of neuraminidase from A/Northern pintail/Washington/40964/2014 influenza virus==
==The crystal structure of neuraminidase from A/Northern pintail/Washington/40964/2014 influenza virus==
<StructureSection load='5huk' size='340' side='right' caption='[[5huk]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
<StructureSection load='5huk' size='340' side='right'caption='[[5huk]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5huk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/northern_pintail/washington/40964/2014(h5n2)) Influenza a virus (a/northern pintail/washington/40964/2014(h5n2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HUK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HUK FirstGlance]. <br>
<table><tr><td colspan='2'>[[5huk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Northern_pintail/Washington/40964/2014(H5N2)) Influenza A virus (A/Northern pintail/Washington/40964/2014(H5N2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HUK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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]] 2.45&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1589662 Influenza A virus (A/Northern pintail/Washington/40964/2014(H5N2))])</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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </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=5huk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5huk OCA], [https://pdbe.org/5huk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5huk RCSB], [https://www.ebi.ac.uk/pdbsum/5huk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5huk ProSAT]</span></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=5huk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5huk OCA], [http://pdbe.org/5huk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5huk RCSB], [http://www.ebi.ac.uk/pdbsum/5huk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5huk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/A0A0C4WXC5_9INFA A0A0C4WXC5_9INFA]] 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 (By similarity).[SAAS:SAAS00234776]  
[https://www.uniprot.org/uniprot/A0A0C4WXC5_9INFA A0A0C4WXC5_9INFA] 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 (By similarity).[SAAS:SAAS00234776]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 20: Line 19:
</div>
</div>
<div class="pdbe-citations 5huk" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5huk" style="background-color:#fffaf0;"></div>
==See Also==
*[[Neuraminidase 3D structures|Neuraminidase 3D structures]]
*[[O-GlcNAcase|O-GlcNAcase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Exo-alpha-sialidase]]
[[Category: Large Structures]]
[[Category: Carney, P J]]
[[Category: Carney PJ]]
[[Category: Chang, J C]]
[[Category: Chang JC]]
[[Category: Guo, Z]]
[[Category: Guo Z]]
[[Category: Stevens, J]]
[[Category: Stevens J]]
[[Category: Yang, H]]
[[Category: Yang H]]
[[Category: H5nx]]
[[Category: Influenza virus]]
[[Category: Neuraminidase]]
[[Category: Viral protein]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA