Database accession: MF7000125
Name: Endophilin-A1 BAR domain (mouse)
PDB ID: 1zww
Experimental method: X-ray (2.30 Å)
Assembly: Homodimer
Source organism: Mus musculus
Primary publication of the structure:
Weissenhorn W
Crystal structure of the endophilin-A1 BAR domain.
(2005) J. Mol. Biol. 351: 653-61
PMID: 16023669
Abstract:
Endophilin has been implicated in the retrieval of membrane via endocytosis of clathrin-coated vesicles, which is crucial for the maintenance of neurotransmitter exocytosis during stimulation; both exocytosis and endocytosis are regulated by intracellular calcium levels. Here, we present the 2.3 A crystal structure of the endophilin-A1 BAR domain, which has been suggested to function in inducing and sensing membrane curvature at the site of endocytosis. Endo-BAR folds into a crescent-shaped dimer composed of two elongated, three-helix bundles. Two additional domains of 30 residues each, inserted into helix 1 at the center of the concave side of the dimer, may interfere with the proposed mode of BAR domain membrane interaction. In addition, the dimer binds 11 divalent cadmium ions in the crystal mostly with typical Ca2+ co-ordination spheres. The endophilin-1A BAR domain thus constitutes a new variant of a BAR domain, and it may link endophilin-1A BAR function to calcium regulation of endocytosis.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
identical protein binding identical protein binding
lipid binding lipid binding
protein kinase binding protein kinase binding
transmembrane transporter binding transmembrane transporter binding
Biological process:
cellular response to brain-derived neurotrophic factor stimulus cellular response to brain-derived neurotrophic factor stimulus
dendrite extension dendrite extension
lipid tube assembly lipid tube assembly
membrane bending membrane bending
membrane tubulation membrane tubulation
neuron projection development neuron projection development
positive regulation of membrane tubulation positive regulation of membrane tubulation
postsynaptic actin cytoskeleton organization postsynaptic actin cytoskeleton organization
regulation of clathrin-dependent endocytosis regulation of clathrin-dependent endocytosis
regulation of receptor internalization regulation of receptor internalization
synaptic vesicle endocytosis synaptic vesicle endocytosis
synaptic vesicle uncoating synaptic vesicle uncoating
vesicle scission vesicle scission
Cellular component:
basal dendrite basal dendrite
cytoplasm cytoplasm
early endosome early endosome
glutamatergic synapse glutamatergic synapse
hippocampal mossy fiber to CA3 synapse hippocampal mossy fiber to CA3 synapse
neuronal cell body neuronal cell body
perinuclear region of cytoplasm perinuclear region of cytoplasm
photoreceptor ribbon synapse photoreceptor ribbon synapse
postsynapse postsynapse
presynapse presynapse
presynaptic cytosol presynaptic cytosol
Schaffer collateral - CA1 synapse Schaffer collateral - CA1 synapse
synapse synapse
synaptic vesicle membrane synaptic vesicle 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: Endophilin-A1
Source organism: Mus musculus
Length: 352 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFATGDSTQPNGGLSHTGTPKPPGVQMDQPCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLHGQSGFFPINYVEILVALPH
UniProtKB AC: Q62420 (positions: 27-246)
Coverage: 62%
Name: Endophilin-A1
Source organism: Mus musculus
Length: 352 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFATGDSTQPNGGLSHTGTPKPPGVQMDQPCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLHGQSGFFPINYVEILVALPH
UniProtKB AC: Q62420 (positions: 28-247)
Coverage: 62%
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 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)
