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4HJ1

Crystal structure of glycoprotein C from Rift Valley Fever Virus (glycosylated)

Summary for 4HJ1
Entry DOI10.2210/pdb4hj1/pdb
Related4HJC
DescriptorENVELOPE GLYCOPROTEIN, beta-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
Functional Keywordsclass ii fusion protein, membrane fusion, viral envelope, viral protein
Biological sourceRift Valley fever virus (RVFV)
Total number of polymer chains4
Total formula weight193289.09
Authors
Dessau, M.,Modis, Y. (deposition date: 2012-10-12, release date: 2013-01-16, Last modification date: 2024-11-27)
Primary citationDessau, M.,Modis, Y.
Crystal structure of glycoprotein C from Rift Valley fever virus.
Proc.Natl.Acad.Sci.USA, 110:1696-1701, 2013
Cited by
PubMed Abstract: Rift Valley fever virus (RVFV), like many other Bunyaviridae family members, is an emerging human and animal pathogen. Bunyaviruses have an outer lipid envelope bearing two glycoproteins, G(N) and G(C), required for cell entry. Bunyaviruses deliver their genome into the host-cell cytoplasm by fusing their envelope with an endosomal membrane. The molecular mechanism of this key entry step is unknown. The crystal structure of RVFV G(C) reveals a class II fusion protein architecture found previously in flaviviruses and alphaviruses. The structure identifies G(C) as the effector of membrane fusion and provides a direct view of the membrane anchor that initiates fusion. A structure of nonglycosylated G(C) reveals an extended conformation that may represent a fusion intermediate. Unanticipated similarities between G(C) and flavivirus envelope proteins reveal an evolutionary link between the two virus families and provide insights into the organization of G(C) in the outer shell of RVFV.
PubMed: 23319635
DOI: 10.1073/pnas.1217780110
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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