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| | <StructureSection load='5jil' size='340' side='right'caption='[[5jil]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='5jil' size='340' side='right'caption='[[5jil]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jil]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rat_coronavirus Rat coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JIL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JIL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jil]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rat_coronavirus Rat coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JIL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JIL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6KL:METHYL+4,5-BIS(ACETYLAMINO)-3,4,5-TRIDEOXY-D-GLYCERO-ALPHA-D-GALACTO-NON-2-ULOPYRANOSIDONIC+ACID'>6KL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.85Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31632 Rat coronavirus])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6KL:METHYL+4,5-BIS(ACETYLAMINO)-3,4,5-TRIDEOXY-D-GLYCERO-ALPHA-D-GALACTO-NON-2-ULOPYRANOSIDONIC+ACID'>6KL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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/Sialate_O-acetylesterase Sialate O-acetylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.53 3.1.1.53] </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=5jil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jil OCA], [https://pdbe.org/5jil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jil RCSB], [https://www.ebi.ac.uk/pdbsum/5jil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jil 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=5jil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jil OCA], [http://pdbe.org/5jil PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jil RCSB], [http://www.ebi.ac.uk/pdbsum/5jil PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jil ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q3HS77_9BETC Q3HS77_9BETC]] May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Seems to be a 'luxury' protein that is not absolutely necessary for virus infection in culture.[RuleBase:RU361278] | + | [https://www.uniprot.org/uniprot/Q3HS77_9BETC Q3HS77_9BETC] May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Seems to be a 'luxury' protein that is not absolutely necessary for virus infection in culture.[RuleBase:RU361278] |
| | <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== |
| - | *[[Hemagglutinin-esterase|Hemagglutinin-esterase]] | + | *[[Hemagglutinin-esterase 3D structures|Hemagglutinin-esterase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Rat coronavirus]] | | [[Category: Rat coronavirus]] |
| - | [[Category: Sialate O-acetylesterase]]
| + | [[Category: Bakkers MJG]] |
| - | [[Category: Bakkers, M J.G]] | + | [[Category: Feitsma LJ]] |
| - | [[Category: Feitsma, L J]] | + | [[Category: Huizinga EG]] |
| - | [[Category: Groot, R J.de]]
| + | [[Category: De Groot RJ]] |
| - | [[Category: Huizinga, E G]] | + | |
| - | [[Category: Coronavirus]] | + | |
| - | [[Category: Esterase]]
| + | |
| - | [[Category: Hemagglutin]]
| + | |
| - | [[Category: Hepatitis virus]]
| + | |
| - | [[Category: Sialic acid]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
Q3HS77_9BETC May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Seems to be a 'luxury' protein that is not absolutely necessary for virus infection in culture.[RuleBase:RU361278]
Publication Abstract from PubMed
Hemagglutinin-esterases (HEs) are bimodular envelope proteins of orthomyxoviruses, toroviruses, and coronaviruses with a carbohydrate-binding "lectin" domain appended to a receptor-destroying sialate-O-acetylesterase ("esterase"). In concert, these domains facilitate dynamic virion attachment to cell-surface sialoglycans. Most HEs (type I) target 9-O-acetylated sialic acids (9-O-Ac-Sias), but one group of coronaviruses switched to using 4-O-Ac-Sias instead (type II). This specificity shift required quasisynchronous adaptations in the Sia-binding sites of both lectin and esterase domains. Previously, a partially disordered crystal structure of a type II HE revealed how the shift in lectin ligand specificity was achieved. How the switch in esterase substrate specificity was realized remained unresolved, however. Here, we present a complete structure of a type II HE with a receptor analog in the catalytic site and identify the mutations underlying the 9-O- to 4-O-Ac-Sia substrate switch. We show that (i) common principles pertaining to the stereochemistry of protein-carbohydrate interactions were at the core of the transition in lectin ligand and esterase substrate specificity; (ii) in consequence, the switch in O-Ac-Sia specificity could be readily accomplished via convergent intramolecular coevolution with only modest architectural changes in lectin and esterase domains; and (iii) a single, inconspicuous Ala-to-Ser substitution in the catalytic site was key to the emergence of the type II HEs. Our findings provide fundamental insights into how proteins "see" sugars and how this affects protein and virus evolution.
Coronavirus receptor switch explained from the stereochemistry of protein-carbohydrate interactions and a single mutation.,Bakkers MJ, Zeng Q, Feitsma LJ, Hulswit RJ, Li Z, Westerbeke A, van Kuppeveld FJ, Boons GJ, Langereis MA, Huizinga EG, de Groot RJ Proc Natl Acad Sci U S A. 2016 May 16. pii: 201519881. PMID:27185912[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bakkers MJ, Zeng Q, Feitsma LJ, Hulswit RJ, Li Z, Westerbeke A, van Kuppeveld FJ, Boons GJ, Langereis MA, Huizinga EG, de Groot RJ. Coronavirus receptor switch explained from the stereochemistry of protein-carbohydrate interactions and a single mutation. Proc Natl Acad Sci U S A. 2016 May 16. pii: 201519881. PMID:27185912 doi:http://dx.doi.org/10.1073/pnas.1519881113
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