4jpr: Difference between revisions
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==Structure of the ASLV fusion subunit core== | ==Structure of the ASLV fusion subunit core== | ||
<StructureSection load='4jpr' size='340' side='right' caption='[[4jpr]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='4jpr' size='340' side='right'caption='[[4jpr]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jpr]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4jpr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rous_sarcoma_virus_(strain_Schmidt-Ruppin_A) Rous sarcoma virus (strain Schmidt-Ruppin A)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JPR FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.001Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jpr OCA], [https://pdbe.org/4jpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jpr RCSB], [https://www.ebi.ac.uk/pdbsum/4jpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jpr ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4jpr" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Aydin | [[Category: Aydin H]] | ||
[[Category: Lee | [[Category: Lee JE]] | ||
[[Category: Smrke | [[Category: Smrke BM]] | ||
Latest revision as of 14:01, 6 November 2024
Structure of the ASLV fusion subunit coreStructure of the ASLV fusion subunit core
Structural highlights
Publication Abstract from PubMedEntry of enveloped viruses into host cells is mediated by their surface envelope glycoproteins (Env). On the surface of the virus, Env is in a metastable, prefusion state, primed to catalyze the fusion of the viral and host membranes. An external trigger is needed to promote the drastic conformational changes necessary for the fusion subunit to fold into the low-energy, 6-helix bundle. These triggers typically facilitate pH-independent entry at the plasma membrane or pH-dependent entry in a low-pH endosomal compartment. The alpha-retrovirus avian sarcoma leukosis virus (ASLV) has a rare, 2-step entry mechanism with both pH-dependent and pH-independent features. Here, we present the 2.0-A-resolution crystal structure of the ASLV transmembrane (TM) fusion protein. Our structural and biophysical studies indicated that unlike other pH-dependent or pH-independent viral TMs, the ASLV fusion subunit is stable irrespective of pH. Two histidine residues (His490 and His492) in the chain reversal region confer stability at low pH. A structural comparison of class I viral fusion proteins suggests that the presence of a positive charge, either a histidine or arginine amino acid, stabilizes a helical dipole moment and is a signature of fusion proteins active at low pH. The structure now reveals key residues and features that explain its 2-step mechanism, and we discuss the implications of the ASLV TM structure in the context of general mechanisms required for membrane fusion.-Aydin, H., Smrke, B.M., Lee, J. E. Structural characterization of a fusion glycoprotein from a retrovirus that undergoes a hybrid 2-step entry mechanism. Structural characterization of a fusion glycoprotein from a retrovirus that undergoes a hybrid 2-step entry mechanism.,Aydin H, Smrke BM, Lee JE FASEB J. 2013 Sep 13. PMID:24036886[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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