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| | ==Crystal structure of Mouse Hepatitis virus strain S Hemagglutinin- esterase== | | ==Crystal structure of Mouse Hepatitis virus strain S Hemagglutinin- esterase== |
| - | <StructureSection load='4c7l' size='340' side='right' caption='[[4c7l]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='4c7l' size='340' side='right'caption='[[4c7l]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4c7l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cvms Cvms]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C7L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4c7l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Murine_hepatitis_virus_strain_S Murine hepatitis virus strain S]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C7L 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c7w|4c7w]]</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=4c7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7l OCA], [http://pdbe.org/4c7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c7l RCSB], [http://www.ebi.ac.uk/pdbsum/4c7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c7l 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=4c7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7l OCA], [https://pdbe.org/4c7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c7l RCSB], [https://www.ebi.ac.uk/pdbsum/4c7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c7l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HEMA_CVMS HEMA_CVMS] Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-4-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. This receptor-destroying activity is important for virus release as it probably helps preventing self-aggregation and ensures the efficient spread of the progeny virus from cell to cell. May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. May become a target for both the humoral and the cellular branches of the immune system.[HAMAP-Rule:MF_04207]<ref>PMID:22291594</ref> |
| | <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/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cvms]] | + | [[Category: Large Structures]] |
| - | [[Category: Huizinga, E G]] | + | [[Category: Murine hepatitis virus strain S]] |
| - | [[Category: Zeng, Q H]] | + | [[Category: Huizinga EG]] |
| - | [[Category: 4-o-acetylated sialic acid]] | + | [[Category: Zeng QH]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Receptor binding]]
| + | |
| - | [[Category: Receptor destroying]]
| + | |
| Structural highlights
4c7l is a 2 chain structure with sequence from Murine hepatitis virus strain S. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.1Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
HEMA_CVMS Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-4-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. This receptor-destroying activity is important for virus release as it probably helps preventing self-aggregation and ensures the efficient spread of the progeny virus from cell to cell. May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. May become a target for both the humoral and the cellular branches of the immune system.[HAMAP-Rule:MF_04207][1]
Publication Abstract from PubMed
The hemagglutinin-esterases (HEs), envelope glycoproteins of corona-, toro- and orthomyxoviruses, mediate reversible virion attachment to O-acetylated sialic acids (O-Ac-Sias). They do so through concerted action of distinct receptor-binding ("lectin") and receptor-destroying sialate O-acetylesterase ("esterase") domains. Most HEs target 9-O-acetylated Sias. In one lineage of murine coronaviruses, however, HE esterase substrate and lectin ligand specificity changed dramatically as these viruses evolved to use 4-O-acetylated Sias instead. Here we present the crystal structure of the lectin domain of mouse hepatitis virus (MHV) strain S HE, resolved both in its native state and in complex with a receptor analogue. The data show that the shift from 9-O- to 4-O-Ac-Sia receptor usage primarily entailed a change in ligand binding topology and, surprisingly, only modest changes in receptor-binding site architecture. Our findings illustrate the ease with which viruses can change receptor-binding specificity with potential consequences for host-, organ and/or cell tropism, and for pathogenesis.
The murine coronavirus hemagglutinin-esterase receptor-binding site: a major shift in ligand specificity through modest changes in architecture.,Langereis MA, Zeng Q, Heesters BA, Huizinga EG, de Groot RJ PLoS Pathog. 2012 Jan;8(1):e1002492. doi: 10.1371/journal.ppat.1002492. Epub 2012, Jan 26. PMID:22291594[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Langereis MA, Zeng Q, Heesters BA, Huizinga EG, de Groot RJ. The murine coronavirus hemagglutinin-esterase receptor-binding site: a major shift in ligand specificity through modest changes in architecture. PLoS Pathog. 2012 Jan;8(1):e1002492. doi: 10.1371/journal.ppat.1002492. Epub 2012, Jan 26. PMID:22291594 doi:http://dx.doi.org/10.1371/journal.ppat.1002492
- ↑ Langereis MA, Zeng Q, Heesters BA, Huizinga EG, de Groot RJ. The murine coronavirus hemagglutinin-esterase receptor-binding site: a major shift in ligand specificity through modest changes in architecture. PLoS Pathog. 2012 Jan;8(1):e1002492. doi: 10.1371/journal.ppat.1002492. Epub 2012, Jan 26. PMID:22291594 doi:http://dx.doi.org/10.1371/journal.ppat.1002492
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