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: 12437927 DOI: 10.1016/S0092-8674(02)01050-4 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.3 Å)

Structure validation