3cl4: Difference between revisions

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-{{Seed}}
-[[Image:3cl4.png|left|200px]]
-<!--
+==Crystal structure of bovine coronavirus hemagglutinin-esterase==
-The line below this paragraph, containing "STRUCTURE_3cl4", creates the "Structure Box" on the page.
+<StructureSection load='3cl4' size='340' side='right'caption='[[3cl4]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3cl4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovine_coronavirus_Mebus Bovine coronavirus Mebus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CL4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CL4 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-{{STRUCTURE_3cl4|  PDB=3cl4  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cl4 OCA], [https://pdbe.org/3cl4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cl4 RCSB], [https://www.ebi.ac.uk/pdbsum/3cl4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cl4 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HEMA_CVBM HEMA_CVBM] 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-9-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. Seems to be a 'luxury' protein that is not absolutely necessary for virus infection in culture. However, its presence in the virus may alter its pathogenicity. May become a target for both the humoral and the cellular branches of the immune system.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cl/3cl4_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cl4 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The hemagglutinin-esterases (HEs) are a family of viral envelope glycoproteins that mediate reversible attachment to O-acetylated sialic acids by acting both as lectins and as receptor-destroying enzymes (RDEs). Related HEs occur in influenza C, toro-, and coronaviruses, apparently as a result of relatively recent lateral gene transfer events. Here, we report the crystal structure of a coronavirus (CoV) HE in complex with its receptor. We show that CoV HE arose from an influenza C-like HE fusion protein (HEF). In the process, HE was transformed from a trimer into a dimer, whereas remnants of the fusion domain were adapted to establish novel monomer-monomer contacts. Whereas the structural design of the RDE-acetylesterase domain remained unaltered, the HE receptor-binding domain underwent remodeling to such extent that the ligand is now bound in opposite orientation. This is surprising, because the architecture of the HEF site was preserved in influenza A HA over a much larger evolutionary distance, a switch in receptor specificity and extensive antigenic variation notwithstanding. Apparently, HA and HEF are under more stringent selective constraints than HE, limiting their exploration of alternative binding-site topologies. We attribute the plasticity of the CoV HE receptor-binding site to evolutionary flexibility conferred by functional redundancy between HE and its companion spike protein S. Our findings offer unique insights into the structural and functional consequences of independent protein evolution after interviral gene exchange and open potential avenues to broad-spectrum antiviral drug design.
-===Crystal structure of bovine coronavirus hemagglutinin-esterase===
+Structure of coronavirus hemagglutinin-esterase offers insight into corona and influenza virus evolution.,Zeng Q, Langereis MA, van Vliet AL, Huizinga EG, de Groot RJ Proc Natl Acad Sci U S A. 2008 Jul 1;105(26):9065-9. Epub 2008 Jun 11. PMID:18550812<ref>PMID:18550812</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3cl4" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_18550812}}, adds the Publication Abstract to the page
+*[[Hemagglutinin-esterase 3D structures|Hemagglutinin-esterase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 18550812 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_18550812}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Bovine coronavirus Mebus]]
-CL4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bovine_coronavirus Bovine coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CL4 OCA].
+[[Category: Large Structures]]
+[[Category: Huizinga EG]]
-==Reference==
+[[Category: Langereis MA]]
-Structure of coronavirus hemagglutinin-esterase offers insight into corona and influenza virus evolution., Zeng Q, Langereis MA, van Vliet AL, Huizinga EG, de Groot RJ, Proc Natl Acad Sci U S A. 2008 Jul 1;105(26):9065-9. Epub 2008 Jun 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18550812 18550812]
+[[Category: Zeng QH]]
-[[Category: Bovine coronavirus]]
+[[Category: De Groot RJ]]
-[[Category: Sialate O-acetylesterase]]
+[[Category: Van Vliet ALW]]
-[[Category: Single protein]]
-[[Category: Groot, R J.de.]]
-[[Category: Huizinga, E G.]]
-[[Category: Langereis, M A.]]
-[[Category: Vliet, A L.W van.]]
-[[Category: Zeng, Q H.]]
-[[Category: Envelope protein]]
-[[Category: Glycoprotein]]
-[[Category: Hemagglutinin]]
-[[Category: Membrane]]
-[[Category: Sgnh-hydrolase fold]]
-[[Category: Swiss roll]]
-[[Category: Transmembrane]]
-[[Category: Virion]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 13 13:45:01 2008''