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2J2Z

X-Ray Structure of the Chaperone PapD in complex with the Pilus terminator subunit PapH at 2.3 Angstrom resolution

Summary for 2J2Z
Entry DOI10.2210/pdb2j2z/pdb
Related1N0L 1PDK 1QPP 1QPX 3DPA
DescriptorCHAPERONE PROTEIN PAPD, PAP FIMBRIAL MINOR PILIN PROTEIN, SULFATE ION, ... (5 entities in total)
Functional Keywordschaperone/surface active protein, periplasmic, pilus termination, immunoglobulin domain, paph, papd, fimbria, chaperone, p5 pocket, chaperone- surface active protein complex, chaperone-surface active protein complex
Biological sourceESCHERICHIA COLI
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Cellular locationPeriplasm: P15319
Secreted: P07111
Total number of polymer chains2
Total formula weight45003.23
Authors
Verger, D.,Miller, E.,Remaut, H.,Waksman, G.,Hultgren, S. (deposition date: 2006-08-17, release date: 2006-11-08, Last modification date: 2024-11-06)
Primary citationVerger, D.,Miller, E.,Remaut, H.,Waksman, G.,Hultgren, S.
Molecular Mechanism of P Pilus Termination in Uropathogenic Escherichia Coli.
Embo Rep., 7:1228-, 2006
Cited by
PubMed Abstract: P pili are important adhesive fibres that are assembled by the conserved chaperone-usher pathway. During pilus assembly, the subunits are incorporated into the growing fibre by the donor-strand exchange mechanism, whereby the beta-strand of the chaperone, which complements the incomplete immunoglobulin fold of each subunit, is displaced by the amino-terminal extension of an incoming subunit in a zip-in-zip-out exchange process that is initiated at the P5 pocket, an exposed hydrophobic pocket in the groove of the subunit. In vivo, termination of P pilus growth requires a specialized subunit, PapH. Here, we show that PapH is incorporated at the base of the growing pilus, where it is unable to undergo donor-strand exchange. This inability is not due to a stronger PapD-PapH interaction, but to a lack of a P5 initiator pocket in the PapH structure, suggesting that PapH terminates pilus growth because it is lacking the initiation point by which donor-strand exchange proceeds.
PubMed: 17082819
DOI: 10.1038/SJ.EMBOR.7400833
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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数据于2024-11-13公开中

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