Database accession: MF7000916
Name: Amphiphysin BAR domain (Drosophila)
PDB ID: 1uru
Experimental method: X-ray (2.60 Å)
Assembly: Homodimer
Source organism: Drosophila melanogaster
Primary publication of the structure:
Peter BJ, Kent HM, Mills IG, Vallis Y, Butler PJ, Evans PR, McMahon HT
BAR domains as sensors of membrane curvature: the amphiphysin BAR structure.
(2004) Science 303: 495-9
PMID: 14645856
Abstract:
The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in amphiphysins from yeast to human and is also found in endophilins and nadrins. We solved the structure of the Drosophila amphiphysin BAR domain. It is a crescent-shaped dimer that binds preferentially to highly curved negatively charged membranes. With its N-terminal amphipathic helix and BAR domain (N-BAR), amphiphysin can drive membrane curvature in vitro and in vivo. The structure is similar to that of arfaptin2, which we find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
phospholipid binding phospholipid binding
Biological process:
exocytosis exocytosis
protein localization protein localization
regulation of muscle contraction regulation of muscle contraction
rhabdomere development rhabdomere development
rhabdomere membrane biogenesis rhabdomere membrane biogenesis
Cellular component:
cleavage furrow cleavage furrow
cytoplasm cytoplasm
organelle organelle
plasma membrane plasma membrane
synapse synapse
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: 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: Amphiphysin
Source organism: Drosophila melanogaster
Length: 602 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMTENKGIMLAKSVQKHAGRAKEKILQNLGKVDRTADEIFDDHLNNFNRQQASANRLQKEFNNYIRCVRAAQAASKTLMDSVCEIYEPQWSGYDALQAQTGASESLWADFAHKLGDQVLIPLNTYTGQFPEMKKKVEKRNRKLIDYDGQRHSFQNLQANANKRKDDVKLTKGREQLEEARRTYEILNTELHDELPALYDSRILFLVTNLQTLFATEQVFHNETAKIYSELEAIVDKLATESQRGSNTLRKQTSNPIKTSSPVQSPVNKLNNANINSNYQNQITTNGGSSLANSPTSTSSSLQEPRFDSVSSTPEPRPESPAAALVSATPSSPVENGVTTKSLERPELSGLNASAKATTTTQTSPTEDKAVVSEAVKPSETEGAAVAASVTPAPPATPAQINGNNNEPSIVKEGGKQPKELPSTTSNAEAAAEAAANNGNSIEEHKQKKLGNDTTVTATETVTVTQHSVTSTDTDNIVTISDTNTDTDTKTSTGTSQKGRPVPVVNRHSVNNLNKNPFEDDDERIYEVPADANTADLPPGVLYRVKATYGYAKEDVDELSFEIGDLIRVIEYDDPEDQEEGWLMGQKEGTNEKGLFPANFTRPI
UniProtKB AC: Q7KLE5 (positions: 26-242)
Coverage: 36%
Name: Amphiphysin
Source organism: Drosophila melanogaster
Length: 602 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMTENKGIMLAKSVQKHAGRAKEKILQNLGKVDRTADEIFDDHLNNFNRQQASANRLQKEFNNYIRCVRAAQAASKTLMDSVCEIYEPQWSGYDALQAQTGASESLWADFAHKLGDQVLIPLNTYTGQFPEMKKKVEKRNRKLIDYDGQRHSFQNLQANANKRKDDVKLTKGREQLEEARRTYEILNTELHDELPALYDSRILFLVTNLQTLFATEQVFHNETAKIYSELEAIVDKLATESQRGSNTLRKQTSNPIKTSSPVQSPVNKLNNANINSNYQNQITTNGGSSLANSPTSTSSSLQEPRFDSVSSTPEPRPESPAAALVSATPSSPVENGVTTKSLERPELSGLNASAKATTTTQTSPTEDKAVVSEAVKPSETEGAAVAASVTPAPPATPAQINGNNNEPSIVKEGGKQPKELPSTTSNAEAAAEAAANNGNSIEEHKQKKLGNDTTVTATETVTVTQHSVTSTDTDNIVTISDTNTDTDTKTSTGTSQKGRPVPVVNRHSVNNLNKNPFEDDDERIYEVPADANTADLPPGVLYRVKATYGYAKEDVDELSFEIGDLIRVIEYDDPEDQEEGWLMGQKEGTNEKGLFPANFTRPI
UniProtKB AC: Q7KLE5 (positions: 26-242)
Coverage: 36%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: N-BAR domain
Evidence level: Direct evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
The human AmphyphisinII/Bin1 and Endophilin BAR domains (N-BARs) display two-state equilibrium unfolding from the dimeric to unfolded monomeric forms (PMID:26368922, PMID:34423187).
Chain A:
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). Download the CIF file (.cif)
Download this entry's XML file (.xml)
Download this entry's JSON file (.json)
