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2W07

Structural determinants of polymerization reactivity of the P pilus adaptor subunit PapF

Summary for 2W07
Entry DOI10.2210/pdb2w07/pdb
DescriptorCHAPERONE PROTEIN PAPD, MINOR PILIN SUBUNIT PAPF, SULFATE ION, ... (4 entities in total)
Functional Keywordsdonor strand complementation, nte, papd, papf, pili, pilin, groove, subunit, immunoglobulin domain, donor-strand exchange, secreted, fimbrium, periplasm, p5 pocket, chaperone, cell adhesion, cell projection, pilus biogenesis, order of assembly, n-terminal extension
Biological sourceESCHERICHIA COLI
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Cellular locationPeriplasm (By similarity): Q1R2W9
Total number of polymer chains2
Total formula weight40548.61
Authors
Verger, D.,Rose, R.J.,Paci, E.,Costakes, G.,Daviter, T.,Hultgren, S.,Remaut, H.,Ashcroft, A.E.,Radford, S.E.,Waksman, G. (deposition date: 2008-08-12, release date: 2008-11-25, Last modification date: 2024-11-06)
Primary citationVerger, D.,Rose, R.J.,Paci, E.,Costakes, G.,Daviter, T.,Hultgren, S.,Remaut, H.,Ashcroft, A.E.,Radford, S.E.,Waksman, G.
Structural Determinants of Polymerization Reactivity of the P Pilus Adaptor Subunit Papf.
Structure, 16:1724-, 2008
Cited by
PubMed Abstract: P pili are important adhesive fibers involved in kidney infection by uropathogenic Escherichia coli. Pilus subunits are characterized by a large groove resulting from lack of a beta strand. Polymerization of pilus subunits occurs via the donor-strand exchange (DSE) mechanism initiated when the N terminus of an incoming subunit interacts with the P5 region/pocket of the previously assembled subunit groove. Here, we solve the structure of the PapD:PapF complex in order to understand why PapF undergoes slow DSE. The structure reveals that the PapF P5 pocket is partially obstructed. MD simulations show this region of PapF is flexible compared with its equivalent in PapH, a subunit that also has an obstructed P5 pocket and is unable to undergo DSE. Using electrospray-ionization mass spectrometry, we show that mutations in the P5 region result in increased DSE rates. Thus, partial obstruction of the P5 pocket serves as a modulating mechanism of DSE.
PubMed: 19000824
DOI: 10.1016/J.STR.2008.08.012
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

227111

數據於2024-11-06公開中

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