Database accession: MF7000694
Name: Mouse PACSIN2 F-BAR domain
PDB ID: 3lll
Experimental method: X-ray (3.30 Å)
Assembly: Homodimer
Source organism: Mus musculus
Primary publication of the structure:
Plomann M, Wittmann JG, Rudolph MG
A hinge in the distal end of the PACSIN 2 F-BAR domain may contribute to membrane-curvature sensing.
(2010) J. Mol. Biol. 400: 129-36
PMID: 20471395
Abstract:
The protein kinase C and casein kinase 2 substrates in neurons (PACSINs) represent a subfamily of membrane-binding proteins characterized by an amino-terminal Bin-Amphiphysin-Rvs (F-BAR) domain. PACSINs link membrane trafficking with actin dynamics and regulate the localization of distinct cargo molecules. The F-BAR domain forms a dimer essential for lipid binding. We have obtained crystals of authentic murine PACSIN 2 that contain an ordered F-BAR domain, indicating that additional domains are flexibly connected to F-BAR. The structure shares similarity to other BAR domains and exhibits special features unique to PACSINs. These include the uneven distribution of charged residues on the concave molecular surface and a so-called wedge loop that is driven into the membrane upon binding of PACSIN. The murine PACSIN 2 F-BAR domain requires dimerization for sensing of curved membranes, and the present structure also provides a mechanism for higher-order oligomer formation. Importantly, comparison of murine with human and Drosophila PACSIN 2 F-BAR domains reveals stark differences in the orientation of distal helical segments leading to a wider crescent shape of murine PACSIN 2. We define hinge residues for these movements that may help PACSINs sense and concomitantly reinforce membrane curvature.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
cytoskeletal protein binding cytoskeletal protein binding
identical protein binding identical protein binding
lipid binding lipid binding
phosphatidic acid binding phosphatidic acid binding
phospholipid binding phospholipid binding
Biological process:
actin cytoskeleton organization actin cytoskeleton organization
caveola assembly caveola assembly
caveolin-mediated endocytosis caveolin-mediated endocytosis
cell projection morphogenesis cell projection morphogenesis
cytoskeleton organization cytoskeleton organization
modulation of chemical synaptic transmission modulation of chemical synaptic transmission
negative regulation of endocytosis negative regulation of endocytosis
plasma membrane tubulation plasma membrane tubulation
protein localization to endosome protein localization to endosome
regulation of endocytosis regulation of endocytosis
signal transduction signal transduction
Cellular component:
caveola caveola
cell-cell junction cell-cell junction
centriolar satellite centriolar satellite
cytoplasm cytoplasm
cytosol cytosol
early endosome early endosome
endosome endosome
glutamatergic synapse glutamatergic synapse
nuclear speck nuclear speck
plasma membrane plasma membrane
recycling endosome membrane recycling endosome membrane
ruffle membrane ruffle 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: Protein kinase C and casein kinase substrate in neurons protein 2
Source organism: Mus musculus
Length: 486 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCGDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWIAVMSEAERVSELHLEVKASLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAHHTACKEEKLAISREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKDKYEKSLKELDQTTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKTIYRELEQSIKAADAVEDLRWFRANHGPGMAMNWPQFEEWSADLNRTLSRREKKKAVDGVTLTGINQTGDQSGQNKPGSNLSVPSNPAQSTQLQSSYNPFEDEDDTGSSISEKEDIKAKNVSSYEKTQTYPTDWSDDESNNPFSSTDANGDSNPFDEDTTSGTEVRVRALYDYEGQEHDELSFKAGDELTKIEDEDEQGWCKGRLDSGQVGLYPANYVEAIQ
UniProtKB AC: Q9WVE8 (positions: 16-302)
Coverage: 59%
Name: Protein kinase C and casein kinase substrate in neurons protein 2
Source organism: Mus musculus
Length: 486 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCGDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWIAVMSEAERVSELHLEVKASLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAHHTACKEEKLAISREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKDKYEKSLKELDQTTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKTIYRELEQSIKAADAVEDLRWFRANHGPGMAMNWPQFEEWSADLNRTLSRREKKKAVDGVTLTGINQTGDQSGQNKPGSNLSVPSNPAQSTQLQSSYNPFEDEDDTGSSISEKEDIKAKNVSSYEKTQTYPTDWSDDESNNPFSSTDANGDSNPFDEDTTSGTEVRVRALYDYEGQEHDELSFKAGDELTKIEDEDEQGWCKGRLDSGQVGLYPANYVEAIQ
UniProtKB AC: Q9WVE8 (positions: 16-302)
Coverage: 59%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: F-BAR domain
Evidence level: Direct evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (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)
