1N0L
Crystal structure of the PapD chaperone (C-terminally 6x histidine-tagged) bound to the PapE pilus subunit (N-terminal-deleted) from uropathogenic E. coli
Summary for 1N0L
Entry DOI | 10.2210/pdb1n0l/pdb |
Related | 1N12 |
Descriptor | Chaperone protein PapD, mature Fimbrial protein PapE (3 entities in total) |
Functional Keywords | immunoglobulin-like fold, donor strand complemenation, donor strand exchange, chaperone priming, pilus fiber assembly, chaperone |
Biological source | Escherichia coli More |
Cellular location | Periplasm: P15319 Secreted: P08407 |
Total number of polymer chains | 4 |
Total formula weight | 80783.00 |
Authors | Sauer, F.G.,Pinkner, J.S.,Waksman, G.,Hultgren, S.J. (deposition date: 2002-10-14, release date: 2002-12-11, Last modification date: 2011-07-13) |
Primary citation | Sauer, F.G.,Pinkner, J.S.,Waksman, G.,Hultgren, S.J. Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation Cell(Cambridge,Mass.), 111:543-551, 2002 Cited by PubMed: 12437927DOI: 10.1016/S0092-8674(02)01050-4 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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