This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5jil

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Crystal structure of rat coronavirus strain New-Jersey Hemagglutinin-Esterase in complex with 4N-acetyl sialic acid

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5jil"

@@ Line 1: / Line 1: @@
 ==Crystal structure of rat coronavirus strain New-Jersey Hemagglutinin-Esterase in complex with 4N-acetyl sialic acid==
-<StructureSection load='5jil' size='340' side='right' caption='[[5jil]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+<StructureSection load='5jil' size='340' side='right'caption='[[5jil]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5jil]] is a 1 chain structure. 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]] 1.85&#8491;</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='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='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>
+<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>
 </table>
 == 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;">
-== 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<ref>PMID:27185912</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5jil" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Hemagglutinin-esterase|Hemagglutinin-esterase]]
+*[[Hemagglutinin-esterase 3D structures|Hemagglutinin-esterase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Sialate O-acetylesterase]]
+[[Category: Large Structures]]
-[[Category: Bakkers, M J.G]]
+[[Category: Rat coronavirus]]
-[[Category: Feitsma, L J]]
+[[Category: Bakkers MJG]]
-[[Category: Groot, R J.de]]
+[[Category: Feitsma LJ]]
-[[Category: Huizinga, E G]]
+[[Category: Huizinga EG]]
-[[Category: Coronavirus]]
+[[Category: De Groot RJ]]
-[[Category: Esterase]]
-[[Category: Hemagglutin]]
-[[Category: Hepatitis virus]]
-[[Category: Sialic acid]]
-[[Category: Viral protein]]

5jil

From Proteopedia

Current revision

Crystal structure of rat coronavirus strain New-Jersey Hemagglutinin-Esterase in complex with 4N-acetyl sialic acid

Structural highlights

Function

See Also

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox