General Information

Database accession: MF7000699

Name: Hof1p F-BAR domain

PDB ID: 4wpe PDBe

Experimental method: X-ray (2.70 Å)

Assembly: Homodimer

Source organism: Saccharomyces cerevisiae

Primary publication of the structure:

Moravcevic K, Alvarado D, Schmitz KR, Kenniston JA, Mendrola JM, Ferguson KM, Lemmon MA
Comparison of Saccharomyces cerevisiae F-BAR domain structures reveals a conserved inositol phosphate binding site.
(2015) Structure 23: 352-63

PMID: 25620000 PubMed

Abstract:

F-BAR domains control membrane interactions in endocytosis, cytokinesis, and cell signaling. Although they are generally thought to bind curved membranes containing negatively charged phospholipids, numerous functional studies argue that differences in lipid-binding selectivities of F-BAR domains are functionally important. Here, we compare membrane-binding properties of the Saccharomyces cerevisiae F-BAR domains in vitro and in vivo. Whereas some F-BAR domains (such as Bzz1p and Hof1p F-BARs) bind equally well to all phospholipids, the F-BAR domain from the RhoGAP Rgd1p preferentially binds phosphoinositides. We determined X-ray crystal structures of F-BAR domains from Hof1p and Rgd1p, the latter bound to an inositol phosphate. The structures explain phospholipid-binding selectivity differences and reveal an F-BAR phosphoinositide binding site that is fully conserved in a mammalian RhoGAP called Gmip and is partly retained in certain other F-BAR domains. Our findings reveal previously unappreciated determinants of F-BAR domain lipid-binding specificity and provide a basis for its prediction from sequence.


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

cytoskeletal protein binding cytoskeletal protein binding GeneOntology

identical protein binding identical protein binding GeneOntology

myosin II heavy chain binding myosin II heavy chain binding GeneOntology

phospholipid binding phospholipid binding GeneOntology

protein-containing complex binding protein-containing complex binding GeneOntology

Biological process:

actin filament bundle assembly actin filament bundle assembly GeneOntology

cytoskeleton organization cytoskeleton organization GeneOntology

mitotic actomyosin contractile ring assembly mitotic actomyosin contractile ring assembly GeneOntology

mitotic actomyosin contractile ring contraction mitotic actomyosin contractile ring contraction GeneOntology

mitotic cytokinesis mitotic cytokinesis GeneOntology

mitotic cytokinetic process mitotic cytokinetic process GeneOntology

negative regulation of actin nucleation negative regulation of actin nucleation GeneOntology

negative regulation of formin-nucleated actin cable assembly negative regulation of formin-nucleated actin cable assembly GeneOntology

primary cell septum biogenesis primary cell septum biogenesis GeneOntology

protein localization to cell division site protein localization to cell division site GeneOntology

regulation of actomyosin contractile ring contraction regulation of actomyosin contractile ring contraction GeneOntology

regulation of cell wall organization or biogenesis regulation of cell wall organization or biogenesis GeneOntology

regulation of cytokinesis regulation of cytokinesis GeneOntology

regulation of mitotic actomyosin contractile ring contraction regulation of mitotic actomyosin contractile ring contraction GeneOntology

Cellular component:

cell cortex cell cortex GeneOntology

cell division site cell division site GeneOntology

cellular bud neck cellular bud neck GeneOntology

cellular bud neck contractile ring cellular bud neck contractile ring GeneOntology

cellular bud neck septin ring cellular bud neck septin ring GeneOntology

cytoplasm cytoplasm GeneOntology

cytoplasmic side of plasma membrane cytoplasmic side of plasma membrane GeneOntology

HICS complex HICS complex GeneOntology

membrane membrane GeneOntology

MIH complex MIH complex GeneOntology

mitotic actomyosin contractile ring, proximal layer mitotic actomyosin contractile ring, proximal layer GeneOntology

plasma membrane plasma membrane GeneOntology

site of polarized growth site of polarized growth GeneOntology

Structure Summary 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


Chain A

Name: Cytokinesis protein 2

Source organism: Saccharomyces cerevisiae

Length: 669 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMSYSYEACFWDPNDNGVNILLGHISQGIRSCDSMILFFKQRSELEKDYARRLGAITGKLDKDIGTNMDYGKLNETFNVVLSVEKARAQSHSKQSEILFRQIYTDTKAFAANLQARYTTLSGKIERLRMDKFNKKKGCEVLQKKLQDAQIRFRDLQLNENNMIGAKRVEHNKRELLKWESNSQEYKVQLDVLKQEYKASQKFWIHEWAQLSCELQEMENARISFLQSKLQQFATSSMETYILEQTKMDMLTNHLNSFTAADEISTFSKENGTGRLKHKTSKGDMNSSANWAQMSSISTTSKKTESYMDNIRKLSSQLKETENKRKLASIDKYEKPLPSPEVTMATQFRNSTPVIRNETKVVANPTLSLRSSPVQLQSNVDDSVLRQKPDKPRPIVGEEQLKPDEDSKNPDEKGLMVHKRNQSLSSPSESSSSNPTDFSHIKKRQSMESMTTSVSSMANSIDDSQRFAKSWNSSNRKRKSMSHLQVPSSASSRSDDGGRTPNSAHNLNEDDYNTRRDTSTSTILFKPPVAVRGTSRGHTHRQSMIMQDSSNPIEDALYEMERIQSSSKPGTKTGNIMDERGVVRDRGITVTLPIVTSEGFPVIEYAKAMYPLIGNEAPGLANFHKGDYLLITEIVNKDWYKGEVYDNDRIDRNHRIGLIPYNFIQLLHQGL

UniProtKB AC: Q05080 (positions: 2-275) UniProt

Coverage: 40%

Chain A-2

Name: Cytokinesis protein 2

Source organism: Saccharomyces cerevisiae

Length: 669 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMSYSYEACFWDPNDNGVNILLGHISQGIRSCDSMILFFKQRSELEKDYARRLGAITGKLDKDIGTNMDYGKLNETFNVVLSVEKARAQSHSKQSEILFRQIYTDTKAFAANLQARYTTLSGKIERLRMDKFNKKKGCEVLQKKLQDAQIRFRDLQLNENNMIGAKRVEHNKRELLKWESNSQEYKVQLDVLKQEYKASQKFWIHEWAQLSCELQEMENARISFLQSKLQQFATSSMETYILEQTKMDMLTNHLNSFTAADEISTFSKENGTGRLKHKTSKGDMNSSANWAQMSSISTTSKKTESYMDNIRKLSSQLKETENKRKLASIDKYEKPLPSPEVTMATQFRNSTPVIRNETKVVANPTLSLRSSPVQLQSNVDDSVLRQKPDKPRPIVGEEQLKPDEDSKNPDEKGLMVHKRNQSLSSPSESSSSNPTDFSHIKKRQSMESMTTSVSSMANSIDDSQRFAKSWNSSNRKRKSMSHLQVPSSASSRSDDGGRTPNSAHNLNEDDYNTRRDTSTSTILFKPPVAVRGTSRGHTHRQSMIMQDSSNPIEDALYEMERIQSSSKPGTKTGNIMDERGVVRDRGITVTLPIVTSEGFPVIEYAKAMYPLIGNEAPGLANFHKGDYLLITEIVNKDWYKGEVYDNDRIDRNHRIGLIPYNFIQLLHQGL

UniProtKB AC: Q05080 (positions: 2-275) UniProt

Coverage: 40%

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 A-2:

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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