General Information

Database accession: MF7000702

Name: Mouse GAS7cb

PDB ID: 6iko PDBe

Experimental method: X-ray (3.76 Å)

Assembly: Homodimer

Source organism: Mus musculus

Primary publication of the structure:

Hanawa-Suetsugu K, Itoh Y, Ab Fatah M, Nishimura T, Takemura K, Takeshita K, Kubota S, Miyazaki N, Wan Mohamad Noor WNI, Inaba T, Nguyen NTH, Hamada-Nakahara S, Oono-Yakura K, Tachikawa M, Iwasaki K, Kohda D, Yamamoto M, Kitao A, Shimada A, Suetsugu S
Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7.
(2019) Nat Commun 10: 4763

PMID: 31628328 PubMed

Abstract:

Phagocytosis is a cellular process for internalization of micron-sized large particles including pathogens. The Bin-Amphiphysin-Rvs167 (BAR) domain proteins, including the FCH-BAR (F-BAR) domain proteins, impose specific morphologies on lipid membranes. Most BAR domain proteins are thought to form membrane invaginations or protrusions by assembling into helical submicron-diameter filaments, such as on clathrin-coated pits, caveolae, and filopodia. However, the mechanism by which BAR domain proteins assemble into micron-scale phagocytic cups was unclear. Here, we show that the two-dimensional sheet-like assembly of Growth Arrest-Specific 7 (GAS7) plays a critical role in phagocytic cup formation in macrophages. GAS7 has the F-BAR domain that possesses unique hydrophilic loops for two-dimensional sheet formation on flat membranes. Super-resolution microscopy reveals the similar assemblies of GAS7 on phagocytic cups and liposomes. The mutations of the loops abolishes both the membrane localization of GAS7 and phagocytosis. Thus, the sheet-like assembly of GAS7 plays a significant role in phagocytosis.


Function and Biology Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown.

Molecular function:

actin filament binding actin filament binding GeneOntology

Biological process:

actin filament bundle assembly actin filament bundle assembly GeneOntology

actin filament polymerization actin filament polymerization GeneOntology

neuron differentiation neuron differentiation GeneOntology

neuron projection morphogenesis neuron projection morphogenesis GeneOntology

regulation of cell shape regulation of cell shape GeneOntology

Cellular component:

actin filament actin filament GeneOntology

cytoplasm cytoplasm GeneOntology

plasma membrane plasma membrane GeneOntology

ruffle ruffle GeneOntology

Structure Summary 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


Chain A

Name: Growth arrest-specific protein 7

Source organism: Mus musculus

Length: 421 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMATALQKPGMVPPPPGEESQTVILPPGWHSYLSPQGRRYYVNTTTNETTWERPSSSPGISASPAPHRSSLPTTVNGYHASGTPAHPPETAHMSLRKSTGDSQNLGSSSPGRKQSKENTITINCVTFPHPDTMPEQQLLKPTEWSYCDYFWADKKDPQGNGTVAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEGSLGEAWAQVKKSLADEAEVHLKFSAKLHSEVEKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLEIKLSNKTEEDIKKARRKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQLRHETDMFNQSTVEPVDQLLRKVDPAKDRELWVREHKTGNIRPVDMEI

UniProtKB AC: Q60780 (positions: 117-419) UniProt

Coverage: 71%

Chain B

Name: Growth arrest-specific protein 7

Source organism: Mus musculus

Length: 421 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMATALQKPGMVPPPPGEESQTVILPPGWHSYLSPQGRRYYVNTTTNETTWERPSSSPGISASPAPHRSSLPTTVNGYHASGTPAHPPETAHMSLRKSTGDSQNLGSSSPGRKQSKENTITINCVTFPHPDTMPEQQLLKPTEWSYCDYFWADKKDPQGNGTVAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEGSLGEAWAQVKKSLADEAEVHLKFSAKLHSEVEKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLEIKLSNKTEEDIKKARRKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQLRHETDMFNQSTVEPVDQLLRKVDPAKDRELWVREHKTGNIRPVDMEI

UniProtKB AC: Q60780 (positions: 118-420) UniProt

Coverage: 71%

Evidence 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:

Related Structure(s) 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).

There are 19 related structures in the MFIB database:






The molecule viewer shows our modified stucture.

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