3sz7

Crystal structure of the Sgt2 TPR domain from Aspergillus fumigatus

spinqualitylabelsall models 3sz7, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3sz7 is a 1 chain structure with sequence from Aspfu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: AFUA_1G09830 (ASPFU) Activity: Phosphoprotein phosphatase, with EC number 3.1.3.16 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The insertion of tail-anchored transmembrane (TA) proteins into the appropriate membrane is a post-translational event that requires stabilization of the transmembrane domain and targeting to the proper destination. Sgt2 is a heat-shock protein cognate (HSC) co-chaperone that preferentially binds endoplasmic reticulum-destined TA proteins and directs them to the GET pathway via Get4 and Get5. Here, we present the crystal structure from a fungal Sgt2 homolog of the tetratrico-repeat (TPR) domain and part of the linker that connects to the C-terminal domain. The linker extends into the two-carboxylate clamp of the TPR domain from a symmetry-related molecule mimicking the binding to HSCs. Based on this structure, we provide biochemical evidence that the Sgt2 TPR domain has the ability to directly bind multiple HSC family members. The structure allows us to propose features involved in this lower specificity relative to other TPR containing co-chaperones. We further show that a dimer of Sgt2 binds a single Get5 and use small angle x-ray scattering to characterize the domain arrangement of Sgt2 in solution. These results allow us to present a structural model of the Sgt2-Get4/Get5-HSC complex. A structural model of the Sgt2 protein and its interactions with chaperones and the Get4/Get5 complex.,Chartron JW, Gonzalez GM, Clemons WM Jr J Biol Chem. 2011 Sep 30;286(39):34325-34. Epub 2011 Aug 10. PMID:21832041 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Small glutamine-rich tetratricopeptide repeat containing protein alpha

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