Database accession: MF7000943
Name: Rubella virus capsid protein (residues 127-277)
PDB ID: 4hbe
Experimental method: X-ray (2.30 Å)
Assembly: Homodimer
Source organism: Rubella virus
Primary publication of the structure:
Mangala Prasad V, Willows SD, Fokine A, Battisti AJ, Sun S, Plevka P, Hobman TC, Rossmann MG
Rubella virus capsid protein structure and its role in virus assembly and infection.
(2013) Proc. Natl. Acad. Sci. U.S.A. 110: 20105-10
PMID: 24282305
Abstract:
Rubella virus (RV) is a leading cause of birth defects due to infectious agents. When contracted during pregnancy, RV infection leads to severe damage in fetuses. Despite its medical importance, compared with the related alphaviruses, very little is known about the structure of RV. The RV capsid protein is an essential structural component of virions as well as a key factor in virus-host interactions. Here we describe three crystal structures of the structural domain of the RV capsid protein. The polypeptide fold of the RV capsid protomer has not been observed previously. Combining the atomic structure of the RV capsid protein with the cryoelectron tomograms of RV particles established a low-resolution structure of the virion. Mutational studies based on this structure confirmed the role of amino acid residues in the capsid that function in the assembly of infectious virions.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
metal ion binding metal ion binding
RNA binding RNA binding
Biological process:
clathrin-dependent endocytosis of virus by host cell clathrin-dependent endocytosis of virus by host cell
fusion of virus membrane with host endosome membrane fusion of virus membrane with host endosome membrane
virion attachment to host cell virion attachment to host cell
Cellular component:
host cell Golgi membrane host cell Golgi membrane
host cell mitochondrion host cell mitochondrion
membrane membrane
T=4 icosahedral viral capsid T=4 icosahedral viral capsid
viral envelope viral envelope
viral nucleocapsid viral nucleocapsid
virion membrane virion membrane
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, B
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: Structural polyprotein
Source organism: Rubella virus
Length: 1063 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMASTTPITMEDLQKALEAQSRALRAGLAAGASQSRRPRPPRQRDSSTSGDDSGRDSGGPRRRRGNRGRGQRKDWSRAPPPPEERQESRSQTPAPKPSRAPPQQPQPPRMQTGRGGSAPRPELGPPTNPFQAAVARGLRPPLHDPDTEAPTEACVTSWLWSEGEGAVFYRVDLHFTNLGTPPLDEDGRWDPALMYNPCGPEPPAHVVRAYNQPAGDVRGVWGKGERTYAEQDFRVGGTRWHRLLRMPVRGLDGDTAPLPPHTTERIETRSARHPWRIRFGAPQAFLAGLLLAAVAVGTARAGLQPRADMAAPPMPPQPPRAHGQHYGHHHHQLPFLGHDGHHGGTLRVGQHHRNASDVLPGHWLQGGWGCYNLSDWHQGTHVCHTKHMDFWCVEHDRPPPATPTSLTTAANSTTAATPATAPPPCHAGLNDSCGGFLSGCGPMRLRHGADTRCGRLICGLSTTAQYPPTRFGCAMRWGLPPWELVVLTARPEDGWTCRGVPAHPGTRCPELVSPMGRATCSPASALWLATANALSLDHAFAAFVLLVPWVLIFMVCRRACRRRGAAAALTAVVLQGYNPPAYGEEAFTYLCTAPGCATQTPVPVRLAGVRFESKIVDGGCFAPWDLEATGACICEIPTDVSCEGLGAWVPTAPCARIWNGTQRACTFWAVNAYSSGGYAQLASYFNPGGSYYKQYHPTACEVEPAFGHSDAACWGFPTDTVMSVFALASYVQHPHKTVRVKFHTETRTVWQLSVAGVSCNVTTEHPFCNTPHGQLEVQVPPDPGDLVEYIMNYTGNQQSRWGLGSPNCHGPDWASPVCQRHSPDCSRLVGATPERPRLRLVDADDPLLRTAPGPGEVWVTPVIGSQARKCGLHIRAGPYGHATVEMPEWIHAHTTSDPWHPPGPLGLKFKTVRPVALPRALAPPRNVRVTGCYQCGTPALVEGLAPGGGNCHLTVNGEDVGAFPPGKFVTAALLNTPPPYQVSCGGESDRASARVIDPAAQSFTGVVYGTHTTAVSETRQTWAEWAAAHWWQLTLGAICALLLAGLLACCAKCLYYLRGAIAPR
UniProtKB AC: P08563 (positions: 150-247)
Coverage: 9%
Name: Structural polyprotein
Source organism: Rubella virus
Length: 1063 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMASTTPITMEDLQKALEAQSRALRAGLAAGASQSRRPRPPRQRDSSTSGDDSGRDSGGPRRRRGNRGRGQRKDWSRAPPPPEERQESRSQTPAPKPSRAPPQQPQPPRMQTGRGGSAPRPELGPPTNPFQAAVARGLRPPLHDPDTEAPTEACVTSWLWSEGEGAVFYRVDLHFTNLGTPPLDEDGRWDPALMYNPCGPEPPAHVVRAYNQPAGDVRGVWGKGERTYAEQDFRVGGTRWHRLLRMPVRGLDGDTAPLPPHTTERIETRSARHPWRIRFGAPQAFLAGLLLAAVAVGTARAGLQPRADMAAPPMPPQPPRAHGQHYGHHHHQLPFLGHDGHHGGTLRVGQHHRNASDVLPGHWLQGGWGCYNLSDWHQGTHVCHTKHMDFWCVEHDRPPPATPTSLTTAANSTTAATPATAPPPCHAGLNDSCGGFLSGCGPMRLRHGADTRCGRLICGLSTTAQYPPTRFGCAMRWGLPPWELVVLTARPEDGWTCRGVPAHPGTRCPELVSPMGRATCSPASALWLATANALSLDHAFAAFVLLVPWVLIFMVCRRACRRRGAAAALTAVVLQGYNPPAYGEEAFTYLCTAPGCATQTPVPVRLAGVRFESKIVDGGCFAPWDLEATGACICEIPTDVSCEGLGAWVPTAPCARIWNGTQRACTFWAVNAYSSGGYAQLASYFNPGGSYYKQYHPTACEVEPAFGHSDAACWGFPTDTVMSVFALASYVQHPHKTVRVKFHTETRTVWQLSVAGVSCNVTTEHPFCNTPHGQLEVQVPPDPGDLVEYIMNYTGNQQSRWGLGSPNCHGPDWASPVCQRHSPDCSRLVGATPERPRLRLVDADDPLLRTAPGPGEVWVTPVIGSQARKCGLHIRAGPYGHATVEMPEWIHAHTTSDPWHPPGPLGLKFKTVRPVALPRALAPPRNVRVTGCYQCGTPALVEGLAPGGGNCHLTVNGEDVGAFPPGKFVTAALLNTPPPYQVSCGGESDRASARVIDPAAQSFTGVVYGTHTTAVSETRQTWAEWAAAHWWQLTLGAICALLLAGLLACCAKCLYYLRGAIAPR
UniProtKB AC: P08563 (positions: 150-247)
Coverage: 9%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Rubella capsid protein
Evidence level: Indirect evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
RV capsid proteins form a tight, disulfide-linked dimer. There is beta sheet augmentation between the monomers. The resultant 10-stranded, left-handed twisted sheet forms a partially open β-barrel with the two helices lying in the center of the barrel. The β-strands A and B from one monomer are inserted into the BH loop of the other monomer, forming a tightly bound dimeric structure consistent with the previous observation that the RV capsid protein forms dimers when isolated from the virion (PMID:24282305).
Chain A:
N/A
Chain B:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). Download the CIF file (.cif)
Download this entry's XML file (.xml)
Download this entry's JSON file (.json)
