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3DPA

CRYSTAL STRUCTURE OF CHAPERONE PROTEIN PAPD REVEALS AN IMMUNOGLOBULIN FOLD

Summary for 3DPA
Entry DOI10.2210/pdb3dpa/pdb
DescriptorCHAPERONE PROTEIN PAPD (1 entity in total)
Functional Keywordschaperone protein
Biological sourceEscherichia coli
Cellular locationPeriplasm : P15319
Total number of polymer chains1
Total formula weight24575.87
Authors
Holmgren, A.,Branden, C.-I. (deposition date: 1991-10-09, release date: 1991-10-15, Last modification date: 2024-02-21)
Primary citationHolmgren, 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: 2478891
DOI: 10.1038/342248a0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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