3DPA
CRYSTAL STRUCTURE OF CHAPERONE PROTEIN PAPD REVEALS AN IMMUNOGLOBULIN FOLD
Summary for 3DPA
| Entry DOI | 10.2210/pdb3dpa/pdb |
| Descriptor | CHAPERONE PROTEIN PAPD (1 entity in total) |
| Functional Keywords | chaperone protein |
| Biological source | Escherichia coli |
| Cellular location | Periplasm : P15319 |
| Total number of polymer chains | 1 |
| Total formula weight | 24575.87 |
| Authors | Holmgren, A.,Branden, C.-I. (deposition date: 1991-10-09, release date: 1991-10-15, Last modification date: 2024-02-21) |
| Primary citation | Holmgren, A.,Branden, C.I. Crystal structure of chaperone protein PapD reveals an immunoglobulin fold. Nature, 342:248-251, 1989 Cited by PubMed Abstract: The chaperone protein PapD mediates assembly of pili in Escherichia coli. Its polypeptide chain folds into two immunoglobulin-type domains that are homologous in sequence to the human lymphocyte differentiation antigen Leu-1/CD5. PubMed: 2478891DOI: 10.1038/342248a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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