General Information

Database accession: MF3140001 Original MFIB entry

Name: Bacteriophage T4 fibritin

PDB ID: 1aa0 PDBe

Experimental method: X-ray (2.20 Å)

Assembly: Homotrimer

Source organism: Enterobacteria phage T4

Primer 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 PubMed

Abstract:

Not available.


Function and Biology 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:

virionGeneOntology

Structure Summary Structural annotations of the participating protein chains.

Entry contents: 3 distinct polypeptide molecules

Chains: A, B, C

Notes: Chains B and C were generated from chain A using the biomatrices described in the original PDB file.

Number of unique protein segments: 1


Chain A

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) UniProt

UniRef90 AC: UniRef90_P10104 (positions: 372-484) UniRef90

Chain B

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) UniProt

UniRef90 AC: UniRef90_P10104 (positions: 372-484) UniRef90

Chain C

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) UniProt

UniRef90 AC: UniRef90_P10104 (positions: 372-484) UniRef90

Evidence Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding.

Evidence level: Direct evidence

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:

None

Chain B:

None

Chain C:

None

The molecule viewer shows our modified stucture.

Download the CIF file (.gz.cif)

Download this entry's XML file (.xml)