3JYZ

Crystal structure of Pseudomonas aeruginosa (strain: Pa110594) typeIV pilin in space group P41212

Summary for 3JYZ

• Entry DOI: 10.2210/pdb3jyz/pdb
• Related: 1A2Y 1DZO 1OQV 1Q5F 1QVE 1ZWT
• Descriptor: Type IV pilin structural subunit, SULFATE ION (3 entities in total)
• Functional Keywords: pila, methylation, structural protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 15535.69

Authors

Nguyen, Y.,Jackson, S.G.,Aidoo, F.,Junop, M.S.,Burrows, L.L. (deposition date: 2009-09-22, release date: 2009-11-24, Last modification date: 2011-07-13)

Primary citation

Nguyen, Y.,Jackson, S.G.,Aidoo, F.,Junop, M.,Burrows, L.L.
Structural characterization of Novel Pseudomonas aeruginosa type IV pilins.
J.Mol.Biol., 395:491-503, 2010

PubMed Abstract: Pseudomonas aeruginosa type IV pili, composed of PilA subunits, are used for attachment and twitching motility on surfaces. P. aeruginosa strains express one of five phylogenetically distinct PilA proteins, four of which are associated with accessory proteins that are involved either in pilin posttranslational modification or in modulation of pilus retraction dynamics. Full understanding of pilin diversity is crucial for the development of a broadly protective pilus-based vaccine. Here, we report the 1.6-A X-ray crystal structure of an N-terminally truncated form of the novel PilA from strain Pa110594 (group V), which represents the first non-group II pilin structure solved. Although it maintains the typical T4a pilin fold, with a long N-terminal alpha-helix and four-stranded antiparallel beta-sheet connected to the C-terminus by a disulfide-bonded loop, the presence of an extra helix in the alphabeta-loop and a disulfide-bonded loop with helical character gives the structure T4b pilin characteristics. Despite the presence of T4b features, the structure of PilA from strain Pa110594 is most similar to the Neisseria gonorrhoeae pilin and is also predicted to assemble into a fiber similar to the GC pilus, based on our comparative pilus modeling. Interactions between surface-exposed areas of the pilin are suggested to contribute to pilus fiber stability. The non-synonymous sequence changes between group III and V pilins are clustered in the same surface-exposed areas, possibly having an effect on accessory protein interactions. However, based on our high-confidence model of group III PilA(PA14), compensatory changes allow for maintenance of a similar shape.

PubMed: 19895819
DOI: 10.1016/j.jmb.2009.10.070

Experimental method

X-RAY DIFFRACTION (1.55 Å)