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| | ==Structural and functional characterization of neuraminidase-like molecule N10 derived from bat influenza A virus== | | ==Structural and functional characterization of neuraminidase-like molecule N10 derived from bat influenza A virus== |
| - | <StructureSection load='4fvk' size='340' side='right' caption='[[4fvk]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='4fvk' size='340' side='right'caption='[[4fvk]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fvk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/little_yellow-shouldered_bat/guatemala/153/2009(h17n10)) Influenza a virus (a/little yellow-shouldered bat/guatemala/153/2009(h17n10))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FVK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fvk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/little_yellow-shouldered_bat/Guatemala/153/2009(H17N10)) Influenza A virus (A/little yellow-shouldered bat/Guatemala/153/2009(H17N10))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FVK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.198Å</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=1129345 Influenza A virus (A/little yellow-shouldered bat/Guatemala/153/2009(H17N10))])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4fvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fvk OCA], [https://pdbe.org/4fvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fvk RCSB], [https://www.ebi.ac.uk/pdbsum/4fvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fvk 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=4fvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fvk OCA], [http://pdbe.org/4fvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fvk RCSB], [http://www.ebi.ac.uk/pdbsum/4fvk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fvk ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/H6QM75_I09A8 H6QM75_I09A8] Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates.[RuleBase:RU361252] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Neuraminidase|Neuraminidase]] | + | *[[Neuraminidase 3D structures|Neuraminidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Exo-alpha-sialidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Gao, G F]] | + | [[Category: Gao GF]] |
| - | [[Category: Li, Q]] | + | [[Category: Li Q]] |
| - | [[Category: Li, Z X]] | + | [[Category: Li ZX]] |
| - | [[Category: Liu, Y]] | + | [[Category: Liu Y]] |
| - | [[Category: Qi, J X]] | + | [[Category: Qi JX]] |
| - | [[Category: Sun, X M]] | + | [[Category: Sun XM]] |
| - | [[Category: Vavricka, C J]] | + | [[Category: Vavricka CJ]] |
| - | [[Category: 6-bladed beta-propeller]]
| + | |
| - | [[Category: Calcium binding]]
| + | |
| - | [[Category: Glycosylation]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Membrane]]
| + | |
| Structural highlights
Function
H6QM75_I09A8 Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates.[RuleBase:RU361252]
Publication Abstract from PubMed
The recent discovery of the unique genome of influenza virus H17N10 in bats raises considerable doubt about the origin and evolution of influenza A viruses. It also identifies a neuraminidase (NA)-like protein, N10, that is highly divergent from the nine other well-established serotypes of influenza A NA (N1-N9). The structural elucidation and functional characterization of influenza NAs have illustrated the complexity of NA structures, thus raising a key question as to whether N10 has a special structure and function. Here the crystal structure of N10, derived from influenza virus A/little yellow-shouldered bat/Guatemala/153/2009 (H17N10), was solved at a resolution of 2.20 A. Overall, the structure of N10 was found to be similar to that of the other known influenza NA structures. In vitro enzymatic assays demonstrated that N10 lacks canonical NA activity. A detailed structural analysis revealed dramatic alterations of the conserved active site residues that are unfavorable for the binding and cleavage of terminally linked sialic acid receptors. Furthermore, an unusual 150-loop (residues 147-152) was observed to participate in the intermolecular polar interactions between adjacent N10 molecules of the N10 tetramer. Our study of influenza N10 provides insight into the structure and function of the sialidase superfamily and sheds light on the molecular mechanism of bat influenza virus infection.
Structural and functional characterization of neuraminidase-like molecule N10 derived from bat influenza A virus.,Li Q, Sun X, Li Z, Liu Y, Vavricka CJ, Qi J, Gao GF Proc Natl Acad Sci U S A. 2012 Nov 13;109(46):18897-902. doi:, 10.1073/pnas.1211037109. Epub 2012 Sep 24. PMID:23012237[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li Q, Sun X, Li Z, Liu Y, Vavricka CJ, Qi J, Gao GF. Structural and functional characterization of neuraminidase-like molecule N10 derived from bat influenza A virus. Proc Natl Acad Sci U S A. 2012 Nov 13;109(46):18897-902. doi:, 10.1073/pnas.1211037109. Epub 2012 Sep 24. PMID:23012237 doi:10.1073/pnas.1211037109
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