1wyy
From Proteopedia
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|PDB= 1wyy |SIZE=350|CAPTION= <scene name='initialview01'>1wyy</scene>, resolution 2.2Å | |PDB= 1wyy |SIZE=350|CAPTION= <scene name='initialview01'>1wyy</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Human SARS coronavirus]) | |GENE= S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Human SARS coronavirus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wyy OCA], [http://www.ebi.ac.uk/pdbsum/1wyy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wyy RCSB]</span> | ||
}} | }} | ||
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[[Category: Rottier, P J.M.]] | [[Category: Rottier, P J.M.]] | ||
[[Category: Vigouroux, A.]] | [[Category: Vigouroux, A.]] | ||
| - | [[Category: CL]] | ||
[[Category: coiled coil]] | [[Category: coiled coil]] | ||
[[Category: membrane fusion]] | [[Category: membrane fusion]] | ||
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[[Category: viral protein]] | [[Category: viral protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:42:48 2008'' |
Revision as of 21:42, 30 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | S (Human SARS coronavirus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Post-fusion hairpin conformation of the sars coronavirus spike glycoprotein
Overview
The coronavirus spike glycoprotein is a class I membrane fusion protein with two characteristic heptad repeat regions (HR1 and HR2) in its ectodomain. Here, we report the X-ray structure of a previously characterized HR1/HR2 complex of the severe acute respiratory syndrome coronavirus spike protein. As expected, the HR1 and HR2 segments are organized in antiparallel orientations within a rod-like molecule. The HR1 helices form an exceptionally long (120 A) internal coiled coil stabilized by hydrophobic and polar interactions. A striking arrangement of conserved asparagine and glutamine residues of HR1 propagates from two central chloride ions, providing hydrogen-bonding "zippers" that strongly constrain the path of the HR2 main chain, forcing it to adopt an extended conformation at either end of a short HR2 alpha-helix.
About this Structure
1WYY is a Single protein structure of sequence from Human sars coronavirus. Full crystallographic information is available from OCA.
Reference
Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein., Duquerroy S, Vigouroux A, Rottier PJ, Rey FA, Bosch BJ, Virology. 2005 May 10;335(2):276-85. PMID:15840526
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