Database accession: MF7000270
Name: FAD-binding domain from mimivirus sulfhydryl oxidase R596
PDB ID: 3gwn
Experimental method: X-ray (1.78 Å)
Assembly: Homodimer
Source organism: Acanthamoeba polyphaga mimivirus
Primary publication of the structure:
Hakim M, Fass D
Dimer interface migration in a viral sulfhydryl oxidase.
(2009) J. Mol. Biol. 391: 758-68
PMID: 19576902
Abstract:
Large double-stranded DNA viruses, including poxviruses and mimiviruses, encode enzymes to catalyze the formation of disulfide bonds in viral proteins produced in the cell cytosol, an atypical location for oxidative protein folding. These viral disulfide catalysts belong to a family of sulfhydryl oxidases that are dimers of a small five-helix fold containing a Cys-X-X-Cys motif juxtaposed to a flavin adenine dinucleotide cofactor. We report that the sulfhydryl oxidase pB119L from African swine fever virus (ASFV) uses for self-assembly surface different from that observed in homologs from mammals, plants, and fungi. Within a protein family, different packing interfaces for the same oligomerization state are extremely rare. We find that the alternate dimerization mode seen in ASFV pB119L is not characteristic of all viral sulfhydryl oxidases, as the flavin-binding domain from a mimivirus sulfhydryl oxidase assumes the same dimer structure as the known eukaryotic enzymes. ASFV pB119L demonstrates the potential of large double-stranded DNA viruses, which have faster mutation rates than their hosts and the tendency to incorporate host genes, to pioneer new protein folds and self-assembly modes.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
flavin adenine dinucleotide binding flavin adenine dinucleotide binding
flavin-dependent sulfhydryl oxidase activity flavin-dependent sulfhydryl oxidase activity
Biological process:
liver development liver development
Cellular component:
virion component virion component
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: Probable FAD-linked sulfhydryl oxidase R596
Source organism: Acanthamoeba polyphaga mimivirus
Length: 292 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSLSKQVVPTHRVEIAPNSESTCKMDHSNYQHNGLITKIWGTAGWTFNHAVTFGYPLNPTSDDKRRYKNYFISLGDVLPCRLCRESYKKFITTGKTALTNEVLRNRHTLTKWFYDVHNAVNNKLEVDYGLSYEDVVNKYESFRAKCGKPVPTVKGCVTPLDHKAFSFKKLYYMDAPIVSLDKVENFVRIARMRGISDKYFCFLELATVLNGDFNELKKQSSWEYRNKYCQKKIRHMRENAIPSIEEQGYWKGTPTIDELKLLLFLCSNLNRTEVNDAINNVERLESTHYIEN
UniProtKB AC: Q5UP54 (positions: 33-144)
Coverage: 38%
Name: Probable FAD-linked sulfhydryl oxidase R596
Source organism: Acanthamoeba polyphaga mimivirus
Length: 292 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSLSKQVVPTHRVEIAPNSESTCKMDHSNYQHNGLITKIWGTAGWTFNHAVTFGYPLNPTSDDKRRYKNYFISLGDVLPCRLCRESYKKFITTGKTALTNEVLRNRHTLTKWFYDVHNAVNNKLEVDYGLSYEDVVNKYESFRAKCGKPVPTVKGCVTPLDHKAFSFKKLYYMDAPIVSLDKVENFVRIARMRGISDKYFCFLELATVLNGDFNELKKQSSWEYRNKYCQKKIRHMRENAIPSIEEQGYWKGTPTIDELKLLLFLCSNLNRTEVNDAINNVERLESTHYIEN
UniProtKB AC: Q5UP54 (positions: 33-144)
Coverage: 38%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: ERV/ALR sulfhydryl oxidase domain
Evidence level: Insufficient evidence (candidate)
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
There is no information on the stability/disorder of the monomeric forms of FAD-linked sulfhydryl oxidases. The wild-type protein is a dimer in solution (analytical equilibrium ultracentrifugation) (PMID:19576902). The, large, hydrophobic interface is made up of two longer, nearly antiparallel helices per monomer that mediate helix packing interactions to form the interface.
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)
