Database accession: MF3140001
Name: Bacteriophage T4 fibritin
PDB ID: 1aa0
Experimental method: X-ray (2.20 Å)
Assembly: Homotrimer
Source organism: Enterobacteria phage T4
Primary publication of the structure:
Tao Y, Strelkov SV, Mesyanzhinov VV, Rossmann MG
Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain.
(1997) Structure 5: 789-98
PMID: 9261070
Abstract:
Not available.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown.Molecular function: not assigned
Biological process: not assigned
Cellular component:
virion component virion component
Structural annotations of the participating protein chains.Entry contents: 3 distinct polypeptide molecules
Chains: A-3, A, A-2
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: Fibritin
Source organism: Enterobacteria phage T4
Length: 487 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMTDIVLNDLPFVDGPPAEGQSRISWIKNGEEILGADTQYGSEGSMNRPTVSVLRNVEVLDKNIGILKTSLETANSDIKTIQGILDVSGDIEALAQIGINKKDISDLKTLTSEHTEILNGTNNTVDSILADIGPFNAEANSVYRTIRNDLLWIKRELGQYTGQDINGLPVVGNPSSGMKHRIINNTDVITSQGIRLSELETKFIESDVGSLTIEVGNLREELGPKPPSFSQNVYSRLNEIDTKQTTVESDISAIKTSIGYPGNNSIITSVNTNTDNIASINLELNQSGGIKQRLTVIETSIGSDDIPSSIKGQIKDNTTSIESLNGIVGENTSSGLRANVSWLNQIVGTDSSGGQPSPPGSLLNRVSTIETSVSGLNNAVQNLQVEIGNNSAGIKGQVVALNTLVNGTNPNGSTVEERGLTNSIKANETNIASVTQEVNTAKGNISSLQGDVQALQEAGYIPEAPRDGQAYVRKDGEWVFLSTFLSPA
UniProtKB AC: P10104 (positions: 372-484)
Coverage: 23%
Name: Fibritin
Source organism: Enterobacteria phage T4
Length: 487 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMTDIVLNDLPFVDGPPAEGQSRISWIKNGEEILGADTQYGSEGSMNRPTVSVLRNVEVLDKNIGILKTSLETANSDIKTIQGILDVSGDIEALAQIGINKKDISDLKTLTSEHTEILNGTNNTVDSILADIGPFNAEANSVYRTIRNDLLWIKRELGQYTGQDINGLPVVGNPSSGMKHRIINNTDVITSQGIRLSELETKFIESDVGSLTIEVGNLREELGPKPPSFSQNVYSRLNEIDTKQTTVESDISAIKTSIGYPGNNSIITSVNTNTDNIASINLELNQSGGIKQRLTVIETSIGSDDIPSSIKGQIKDNTTSIESLNGIVGENTSSGLRANVSWLNQIVGTDSSGGQPSPPGSLLNRVSTIETSVSGLNNAVQNLQVEIGNNSAGIKGQVVALNTLVNGTNPNGSTVEERGLTNSIKANETNIASVTQEVNTAKGNISSLQGDVQALQEAGYIPEAPRDGQAYVRKDGEWVFLSTFLSPA
UniProtKB AC: P10104 (positions: 372-484)
Coverage: 23%
Name: Fibritin
Source organism: Enterobacteria phage T4
Length: 487 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMTDIVLNDLPFVDGPPAEGQSRISWIKNGEEILGADTQYGSEGSMNRPTVSVLRNVEVLDKNIGILKTSLETANSDIKTIQGILDVSGDIEALAQIGINKKDISDLKTLTSEHTEILNGTNNTVDSILADIGPFNAEANSVYRTIRNDLLWIKRELGQYTGQDINGLPVVGNPSSGMKHRIINNTDVITSQGIRLSELETKFIESDVGSLTIEVGNLREELGPKPPSFSQNVYSRLNEIDTKQTTVESDISAIKTSIGYPGNNSIITSVNTNTDNIASINLELNQSGGIKQRLTVIETSIGSDDIPSSIKGQIKDNTTSIESLNGIVGENTSSGLRANVSWLNQIVGTDSSGGQPSPPGSLLNRVSTIETSVSGLNNAVQNLQVEIGNNSAGIKGQVVALNTLVNGTNPNGSTVEERGLTNSIKANETNIASVTQEVNTAKGNISSLQGDVQALQEAGYIPEAPRDGQAYVRKDGEWVFLSTFLSPA
UniProtKB AC: P10104 (positions: 372-484)
Coverage: 23%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: -
Evidence level: Direct evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
The foldon domain folds into a trimeric beta-propeller structure and undergoes a two-state unfolding transition from folded trimer to unfolded monomers (PMID:15033360). The other subunits in the structure are bound via coiled coil interactions (PMID:9261070). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.
Chain A:
N/A
Chain A-3:
N/A
Chain A-2:
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). No related structure was found in the MFIB database.
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