4NWY
Crystal structure of the b' domain of human protein disulfide isomerase-like protein of the testis (PDILT)
Summary for 4NWY
| Entry DOI | 10.2210/pdb4nwy/pdb |
| Descriptor | Protein disulfide-isomerase-like protein of the testis, FORMIC ACID (3 entities in total) |
| Functional Keywords | thioredoxin-like fold, substrate-binding domain, endoplasmic reticulum, isomerase |
| Biological source | Homo sapiens (human) |
| Cellular location | Endoplasmic reticulum: Q8N807 |
| Total number of polymer chains | 4 |
| Total formula weight | 62366.69 |
| Authors | Bastos-Aristizabal, S.,Kozlov, G.,Gehring, K. (deposition date: 2013-12-07, release date: 2014-04-02, Last modification date: 2023-09-20) |
| Primary citation | Bastos-Aristizabal, S.,Kozlov, G.,Gehring, K. Structure of the substrate-binding b' domain of the Protein disulfide isomerase-like protein of the testis. Sci Rep, 4:4464-4464, 2014 Cited by PubMed Abstract: Protein Disulfide Isomerase-Like protein of the Testis (PDILT) is a testis-specific member of the PDI family. PDILT displays similar domain architecture to PDIA1, the founding member of this protein family, but lacks catalytic cysteines needed for oxidoreduction reactions. This suggests special importance of chaperone activity of PDILT, but how it recognizes misfolded protein substrates is unknown. Here, we report the high-resolution crystal structure of the b' domain of human PDILT. The structure reveals a conserved hydrophobic pocket, which is likely a principal substrate-binding site in PDILT. In the crystal, this pocket is occupied by side chains of tyrosine and tryptophan residues from another PDILT molecule, suggesting a preference for binding exposed aromatic residues in protein substrates. The lack of interaction of the b' domain with the P-domains of calreticulin-3 and calmegin hints at a novel way of interaction between testis-specific lectin chaperones and PDILT. Further studies of this recently discovered PDI member would help to understand the important role that PDILT plays in the differentiation and maturation of spermatozoids. PubMed: 24662985DOI: 10.1038/srep04464 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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