3jzz

Crystal structure of Pseudomonas aeruginosa (strain: Pa110594) typeIV pilin in space group P212121Crystal structure of Pseudomonas aeruginosa (strain: Pa110594) typeIV pilin in space group P212121

Structural highlights 3jzz is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.597Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8KQ36_PSEAI Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural characterization of novel Pseudomonas aeruginosa type IV pilins.,Nguyen Y, Jackson SG, Aidoo F, Junop M, Burrows LL J Mol Biol. 2010 Jan 22;395(3):491-503. Epub 2009 Nov 4. PMID:19895819 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pilin 3D structures

spinqualitylabelsall models 3jzz, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image