Database accession: MF7000954
Name: Homodimerization domain of Sgt2
PDB ID: 2lxb
Experimental method: NMR
Assembly: Homodimer
Source organism: Saccharomyces cerevisiae
Primary publication of the structure:
Chartron JW, VanderVelde DG, Clemons WM
Structures of the Sgt2/SGTA dimerization domain with the Get5/UBL4A UBL domain reveal an interaction that forms a conserved dynamic interface.
(2012) Cell Rep 2: 1620-32
PMID: 23142665
Abstract:
In the cytoplasm, the correct delivery of membrane proteins is an essential and highly regulated process. The posttranslational targeting of the important tail-anchor membrane (TA) proteins has recently been under intense investigation. A specialized pathway, called the guided entry of TA proteins (GET) pathway in yeast and the transmembrane domain recognition complex (TRC) pathway in vertebrates, recognizes endoplasmic-reticulum-targeted TA proteins and delivers them through a complex series of handoffs. An early step is the formation of a complex between Sgt2/SGTA, a cochaperone with a presumed ubiquitin-like-binding domain (UBD), and Get5/UBL4A, a ubiquitin-like domain (UBL)-containing protein. We structurally characterize this UBD/UBL interaction for both yeast and human proteins. This characterization is supported by biophysical studies that demonstrate that complex formation is mediated by electrostatics, generating an interface that has high-affinity with rapid kinetics. In total, this work provides a refined model of the interplay of Sgt2 homologs in TA targeting.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
identical protein binding identical protein binding
molecular adaptor activity molecular adaptor activity
Biological process:
post-translational protein targeting to endoplasmic reticulum membrane post-translational protein targeting to endoplasmic reticulum membrane
response to heat response to heat
Cellular component:
cytoplasm cytoplasm
cytosol cytosol
membrane membrane
TRC complex TRC complex
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: Small glutamine-rich tetratricopeptide repeat-containing protein 2
Source organism: Saccharomyces cerevisiae
Length: 346 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSASKEEIAALIVNYFSSIVEKKEISEDGADSLNVAMDCISEAFGFEREAVSGILGKSEFKGQHLADILNSASRVPESNKKDDAENVEINIPEDDAETKAKAEDLKMQGNKAMANKDYELAINKYTEAIKVLPTNAIYYANRAAAHSSLKEYDQAVKDAESAISIDPSYFRGYSRLGFAKYAQGKPEEALEAYKKVLDIEGDNATEAMKRDYESAKKKVEQSLNLEKTVPEQSRDADVDASQGASAGGLPDLGSLLGGGLGGLMNNPQLMQAAQKMMSNPGAMQNIQKMMQDPSIRQMAEGFASGGGTPNLSDLMNNPALRNMAGNLFGGAGAQSTDETPDNENKQ
UniProtKB AC: Q12118 (positions: 2-72)
Coverage: 20%
Name: Small glutamine-rich tetratricopeptide repeat-containing protein 2
Source organism: Saccharomyces cerevisiae
Length: 346 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSASKEEIAALIVNYFSSIVEKKEISEDGADSLNVAMDCISEAFGFEREAVSGILGKSEFKGQHLADILNSASRVPESNKKDDAENVEINIPEDDAETKAKAEDLKMQGNKAMANKDYELAINKYTEAIKVLPTNAIYYANRAAAHSSLKEYDQAVKDAESAISIDPSYFRGYSRLGFAKYAQGKPEEALEAYKKVLDIEGDNATEAMKRDYESAKKKVEQSLNLEKTVPEQSRDADVDASQGASAGGLPDLGSLLGGGLGGLMNNPQLMQAAQKMMSNPGAMQNIQKMMQDPSIRQMAEGFASGGGTPNLSDLMNNPALRNMAGNLFGGAGAQSTDETPDNENKQ
UniProtKB AC: Q12118 (positions: 2-72)
Coverage: 20%
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:
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)
