5xf7 | pdb_00005xf7

Crystal structure of human protein disulfide isomerase-like protein of the testis

spinqualitylabelsall models 5xf7, resolution 2.38Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xf7 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: PDILT (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PDILT_HUMAN] Probable redox-inactive chaperone involved in spermatogenesis. Publication Abstract from PubMed Protein disulfide isomerase-like protein of the testis (PDILT), a member of the protein disulfide isomerase (PDI) family is a chaperone essential for the folding of spermatogenesis-specific proteins in male postmeiotic germ cells. However, the structural mechanisms that regulate the chaperone function of PDILT are unknown. Here, we report the structures of human PDILT (hPDILT) determined by X-ray crystallography to 2.4 angstrom resolution and small-angle X-ray scattering (SAXS). Distinct from previously reported U-like structures of related PDI family proteins, our structures revealed that hPDILT folds into a compact L-like structure in crystals and into an extended chain-like structure in solution. The hydrophobic regions and the hydrophobic pockets in hPDILT, which are important for substrate recognition, were clearly delineated in the crystal structure. Moreover, our results of the SAXS analysis and of structure-based substitutions and truncations indicated that the C-terminal tail in hPDILT is required for suppression of aggregation of denatured proteins, suggesting that the tail is crucial for the chaperone activity of PDILT. Taken together, our findings have identified the critical regions and conformational changes of PDILT that enable and control its activity. These results advance our understanding of the structural mechanisms involved in the chaperone activity of PDILT. Crystal and solution structures of human protein disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity.,Li H, Yang K, Wang W, Niu Y, Li J, Dong Y, Liu Y, Wang CC, Wang L, Liang H J Biol Chem. 2017 Dec 4. pii: M117.797290. doi: 10.1074/jbc.M117.797290. PMID:29203529 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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