4ASW: Structure of the complex between the N-terminal dimerisation domain of Sgt2 and the UBL domain of Get5

Small, glutamine-rich, tetratricopeptide repeat protein 2 (Sgt2) is the first known port of call for many newly synthesized tail-anchored (TA) proteins released from the ribosome and destined for the GET (Guided Entry of TA proteins) pathway. This leads them to the residential membrane of the endoplasmic reticulum via an alternative to the cotranslational, signal recognition particle-dependent mechanism that their topology denies them. In yeast, the first stage of the GET pathway involves Sgt2 passing TA proteins on to the Get4/Get5 complex through a direct interaction between the N-terminal (NT) domain of Sgt2 and the ubiquitin-like (UBL) domain of Get5. Here we characterize this interaction at a molecular level by solving both a solution structure of Sgt2_NT, which adopts a unique helical fold, and a crystal structure of the Get5_UBL. Furthermore, using reciprocal chemical shift perturbation data and experimental restraints, we solve a structure of the Sgt2_NT/Get5_UBL complex, validate it via site-directed mutagenesis, and empirically determine its stoichiometry using relaxation experiments and isothermal titration calorimetry. Taken together, these data provide detailed structural information about the interaction between two key players in the coordinated delivery of TA protein substrates into the GET pathway.
PDB ID: 4ASWDownload
MMDB ID: 145326
PDB Deposition Date: 2012/5/3
Updated in MMDB: 2016/12
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 4ASW: trimeric; determined by software (PISA)
Molecular Components in 4ASW
Label Count Molecule
Proteins (3 molecules)
Small Glutamine-rich Tetratricopeptide Repeat-containing Protein 2(Gene symbol: SGT2)
Molecule annotation
Ubiquitin-like Protein Mdy2(Gene symbol: MDY2)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB