General Information

Database accession: MF7000956

Name: N-terminal domain of SGTA

PDB ID: 4cpg PDBe

Experimental method: NMR

Assembly: Homodimer

Source organism: Homo sapiens

Primary publication of the structure:

Darby JF, Krysztofinska EM, Simpson PJ, Simon AC, Leznicki P, Sriskandarajah N, Bishop DS, Hale LR, Alfano C, Conte MR, Martínez-Lumbreras S, Thapaliya A, High S, Isaacson RL
Solution structure of the SGTA dimerisation domain and investigation of its interactions with the ubiquitin-like domains of BAG6 and UBL4A.
(2014) PLoS ONE 9: e113281

PMID: 25415308 PubMed

Abstract:

Not available.


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

Molecular function:

BAT3 complex binding BAT3 complex binding GeneOntology

identical protein binding identical protein binding GeneOntology

molecular adaptor activity molecular adaptor activity GeneOntology

Biological process:

ERAD pathway ERAD pathway GeneOntology

negative regulation of ERAD pathway negative regulation of ERAD pathway GeneOntology

negative regulation of ubiquitin-dependent protein catabolic process negative regulation of ubiquitin-dependent protein catabolic process GeneOntology

positive regulation of ERAD pathway positive regulation of ERAD pathway GeneOntology

positive regulation of ubiquitin-dependent protein catabolic process positive regulation of ubiquitin-dependent protein catabolic process GeneOntology

post-translational protein targeting to endoplasmic reticulum membrane post-translational protein targeting to endoplasmic reticulum membrane GeneOntology

tail-anchored membrane protein insertion into ER membrane tail-anchored membrane protein insertion into ER membrane GeneOntology

Cellular component:

cytoplasm cytoplasm GeneOntology

cytosol cytosol GeneOntology

membrane membrane GeneOntology

nucleus nucleus GeneOntology

TRC complex TRC complex 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: Small glutamine-rich tetratricopeptide repeat-containing protein alpha

Source organism: Homo sapiens

Length: 313 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMDNKKRLAYAIIQFLHDQLRHGGLSSDAQESLEVAIQCLETAFGVTVEDSDLALPQTLPEIFEAAATGKEMPQDLRSPARTPPSEEDSAEAERLKTEGNEQMKVENFEAAVHFYGKAIELNPANAVYFCNRAAAYSKLGNYAGAVQDCERAICIDPAYSKAYGRMGLALSSLNKHVEAVAYYKKALELDPDNETYKSNLKIAELKLREAPSPTGGVGSFDIAGLLNNPGFMSMASNLMNNPQIQQLMSGMISGGNNPLGTPGTSPSQNDLASLIQAGQQFAQQMQQQNPELIEQLRSQIRSRTPSASNDDQQE

UniProtKB AC: O43765 (positions: 1-69) UniProt

Coverage: 22%

Chain B

Name: Small glutamine-rich tetratricopeptide repeat-containing protein alpha

Source organism: Homo sapiens

Length: 313 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMDNKKRLAYAIIQFLHDQLRHGGLSSDAQESLEVAIQCLETAFGVTVEDSDLALPQTLPEIFEAAATGKEMPQDLRSPARTPPSEEDSAEAERLKTEGNEQMKVENFEAAVHFYGKAIELNPANAVYFCNRAAAYSKLGNYAGAVQDCERAICIDPAYSKAYGRMGLALSSLNKHVEAVAYYKKALELDPDNETYKSNLKIAELKLREAPSPTGGVGSFDIAGLLNNPGFMSMASNLMNNPQIQQLMSGMISGGNNPLGTPGTSPSQNDLASLIQAGQQFAQQMQQQNPELIEQLRSQIRSRTPSASNDDQQE

UniProtKB AC: O43765 (positions: 1-69) UniProt

Coverage: 22%

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: Homodimerisation domain of SGTA

Evidence level: Indirect evidence

Evidence coverage: The full structure participates in mutual synergistic folding.

Complex Evidence:

The dimer interface is highly hydrophobic, the hydrophobic core is contributed by both monomers, mutations introduced to block dimer formation yielded no soluble protein (PMID:23297211).

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 3 related structures in the MFIB database:






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