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==Crystal structure of Mouse Hepatitis virus strain S Hemagglutinin- esterase in complex with 4-O-acetylated sialic acid== | |||
<StructureSection load='4c7w' size='340' side='right' caption='[[4c7w]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4c7w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Murine_hepatitis_virus Murine hepatitis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C7W 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=SIO:METHYL+4,9-DI-O-ACETYL-5-(ACETYLAMINO)-3,5-DIDEOXY-D-GLYCERO-ALPHA-D-GALACTO-NON-2-ULOPYRANOSIDONIC+ACID'>SIO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c7l|4c7l]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c7w RCSB], [http://www.ebi.ac.uk/pdbsum/4c7w PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:22291594</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
==See Also== | |||
*[[Hemagglutinin-esterase|Hemagglutinin-esterase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Murine hepatitis virus]] | [[Category: Murine hepatitis virus]] | ||
[[Category: Sialate O-acetylesterase]] | [[Category: Sialate O-acetylesterase]] | ||
[[Category: Huizinga, E G | [[Category: Huizinga, E G]] | ||
[[Category: Zeng, Q H | [[Category: Zeng, Q H]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Receptor binding]] | [[Category: Receptor binding]] | ||
[[Category: Receptor destroying]] | [[Category: Receptor destroying]] | ||
Revision as of 12:37, 21 December 2014
Crystal structure of Mouse Hepatitis virus strain S Hemagglutinin- esterase in complex with 4-O-acetylated sialic acidCrystal structure of Mouse Hepatitis virus strain S Hemagglutinin- esterase in complex with 4-O-acetylated sialic acid
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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