Database accession: MF7000695
Name: Mouse PACSIN3 BAR domain, mutant
PDB ID: 3m3w
Experimental method: X-ray (2.60 Å)
Assembly: Homodimer
Source organism: Mus musculus
Primary publication of the structure:
Bai X, Meng G, Luo M, Zheng X
Rigidity of wedge loop in PACSIN 3 protein is a key factor in dictating diameters of tubules.
(2012) J. Biol. Chem. 287: 22387-96
PMID: 22573331
Abstract:
BAR (Bin/amphiphysin/Rvs) domain-containing proteins participate in cellular membrane remodeling. The F-BAR proteins normally generate low curvature tubules. However, in the PACSIN subfamily, the F-BAR domain from PACSIN 1 and 2 can induce both high and low curvature tubules. We found that unlike PACSIN 1 and 2, PACSIN 3 could only induce low curvature tubules. To elucidate the key factors that dictate the tubule curvature, crystal structures of all three PACSIN F-BAR domains were determined. A novel type of lateral interaction mediated by a wedge loop is observed between the F-BAR neighboring dimers. Comparisons of the structures of PACSIN 3 with PACSIN 1 and 2 indicate that the wedge loop of PACSIN 3 is more rigid, which influences the lateral interactions between assembled dimers. We further identified the residues that affect the rigidity of the loop by mutagenesis and determined the structures of two PACSIN 3 wedge loop mutants. Our results suggest that the rigidity-mediated conformations of the wedge loop correlate well with the various crystal packing modes and membrane tubulations. Thus, the rigidity of the wedge loop is a key factor in dictating tubule diameters.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
calcium channel inhibitor activity calcium channel inhibitor activity
cytoskeletal protein binding cytoskeletal protein binding
identical protein binding identical protein binding
lipid binding lipid binding
phospholipid binding phospholipid binding
Biological process:
cytoskeleton organization cytoskeleton organization
endocytosis endocytosis
negative regulation of calcium ion transport negative regulation of calcium ion transport
negative regulation of endocytosis negative regulation of endocytosis
plasma membrane tubulation plasma membrane tubulation
positive regulation of membrane protein ectodomain proteolysis positive regulation of membrane protein ectodomain proteolysis
regulation of endocytosis regulation of endocytosis
Cellular component:
cytoplasm cytoplasm
cytosol cytosol
endosome endosome
plasma membrane plasma 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 II substrate protein 3
Source organism: Mus musculus
Length: 424 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMAPEEDAGGEVLGGSFWEAGNYRRTVQRVEDGHRLCGDLVSCFQERARIEKAYAQQLADWARKWRGAVEKGPQYGTLEKAWHAFFTAAERLSELHLEVREKLHGPDSERVRTWQRGAFHRPVLGGFRESRAAEDGFRKAQKPWLKRLKEVEASKKSYHTARKDEKTAQTRESHAKADSSMSQEQLRKLQERVGRCTKEAEKMKTQYEQTLAELNRYTPRYMEDMEQAFESCQAAERQRLLFFKDVLLTLHQHLDLSSSDKFHELHRDLQQSIEAASDEEDLRWWRSTHGPGMAMNWPQFEEWSLDTQRAISRKEKGGRSPDEVTLTSIVPTRDGTAPPPQSPSSPGSGQDEDWSDEESPRKVATGVRVRALYDYAGQEADELSFRAGEELLKMSEEDEQGWCQGQLQSGRIGLYPANYVECVGA
UniProtKB AC: Q99JB8 (positions: 14-301)
Coverage: 67%
Name: Protein kinase C and casein kinase II substrate protein 3
Source organism: Mus musculus
Length: 424 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMAPEEDAGGEVLGGSFWEAGNYRRTVQRVEDGHRLCGDLVSCFQERARIEKAYAQQLADWARKWRGAVEKGPQYGTLEKAWHAFFTAAERLSELHLEVREKLHGPDSERVRTWQRGAFHRPVLGGFRESRAAEDGFRKAQKPWLKRLKEVEASKKSYHTARKDEKTAQTRESHAKADSSMSQEQLRKLQERVGRCTKEAEKMKTQYEQTLAELNRYTPRYMEDMEQAFESCQAAERQRLLFFKDVLLTLHQHLDLSSSDKFHELHRDLQQSIEAASDEEDLRWWRSTHGPGMAMNWPQFEEWSLDTQRAISRKEKGGRSPDEVTLTSIVPTRDGTAPPPQSPSSPGSGQDEDWSDEESPRKVATGVRVRALYDYAGQEADELSFRAGEELLKMSEEDEQGWCQGQLQSGRIGLYPANYVECVGA
UniProtKB AC: Q99JB8 (positions: 14-302)
Coverage: 68%
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)
