1QPP

CRYSTAL STRUCTURES OF SELF CAPPING PAPD CHAPERONE HOMODIMERS

1QPP の概要

• エントリーDOI: 10.2210/pdb1qpp/pdb
• 関連するPDBエントリー: 1QPX 3dpa
• 分子名称: PAPD CHAPERONE (1 entity in total)
• 機能のキーワード: beta barrel, immunoglobulin fold chaperone, chaperone
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm : P15319
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48979.51

構造登録者

Hung, D.L.,Pinkner, J.S.,Knight, S.D.,Hultgren, S.J. (登録日: 1999-05-28, 公開日: 1999-07-07, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.6 Å)