1QPX

CRYSTAL STRUCTURES OF SELF-CAPPING PAPD CHAPERONE HOMODIMERS

Summary for 1QPX

• Entry DOI: 10.2210/pdb1qpx/pdb
• Related: 1QPP 3dpa
• Descriptor: PAPD CHAPERONE (2 entities in total)
• Functional Keywords: beta barrel, immunoglobulin fold, chaperone
• Biological source: Escherichia coli
• Cellular location: Periplasm : P15319
• Total number of polymer chains: 2
• Total formula weight: 49073.72

Authors

Hung, D.L.,Pinkner, J.S.,Knight, S.D.,Hultgren, S.J. (deposition date: 1999-05-31, release date: 1999-07-07, Last modification date: 2024-11-06)

Primary citation

Hung, D.L.,Pinkner, J.S.,Knight, S.D.,Hultgren, S.J.
Structural basis of chaperone self-capping in P pilus biogenesis.
Proc.Natl.Acad.Sci.USA, 96:8178-8183, 1999

PubMed Abstract: PapD is an immunoglobulin-like chaperone that mediates the assembly of P pili in uropathogenic strains of Escherichia coli. It binds and caps interactive surfaces on pilus subunits to prevent their premature associations in the periplasm. We elucidated the structural basis of a mechanism whereby PapD also interacts with itself, capping its own subunit binding surface. Crystal structures of dimeric forms of PapD revealed that this self-capping mechanism involves a rearrangement and ordering of the C2-D2 and F1-G1 loops upon dimerization which might ensure that a stable dimer is not formed in solution in spite of a relatively large dimer interface. An analysis of site directed mutations revealed that chaperone dimerization requires the same surface that is otherwise used to bind subunits.

PubMed: 10393968
DOI: 10.1073/pnas.96.14.8178

Experimental method

X-RAY DIFFRACTION (2.4 Å)