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Literature DB >> 17012803

Crystallization and preliminary X-ray diffraction analysis of Salmonella typhi PilS.

Asha M Balakrishna¹, Yvonne Yih-Wan Tan, Henry Yu-Keung Mok, Anand M Saxena, Kunchithapadam Swaminathan.

Abstract

The structure determination of PilS, a type IV pilin, by X-ray crystallography is reported. The recombinant protein from Salmonella typhi was overexpressed, purified and crystallized. The crystals belong to space group P2(1)2(1)2, with unit-cell parameters a = 77.88, b = 114.53, c = 31.75 A. The selenomethionine derivative of the PilS protein was overexpressed, purified and crystallized in the same space group. Data sets have been collected to 2.1 A resolution from the selenomethionine-derivative crystal using synchrotron radiation for multiwavelength anomalous dispersion (MAD) phasing.

Entities: Chemical Species

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Year: 2006 PMID： 17012803 PMCID： PMC2225195 DOI： 10.1107/S174430910603661X

Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091

13 in total

1. A HEX-1 crystal lattice required for Woronin body function in Neurospora crassa.

Authors: Ping Yuan; Gregory Jedd; Desigan Kumaran; Subramanyam Swaminathan; Helen Shio; David Hewitt; Nam-Hai Chua; Kunchithapadam Swaminathan
Journal: Nat Struct Biol Date: 2003-04

Review 2. Type IV pilus structure and bacterial pathogenicity.

Authors: Lisa Craig; Michael E Pique; John A Tainer
Journal: Nat Rev Microbiol Date: 2004-05 Impact factor: 60.633

3. Processing of X-ray diffraction data collected in oscillation mode.

Authors: Z Otwinowski; W Minor
Journal: Methods Enzymol Date: 1997 Impact factor: 1.600

4. Solvent content of protein crystals.

Authors: B W Matthews
Journal: J Mol Biol Date: 1968-04-28 Impact factor: 5.469

5. Crystal structure of Pseudomonas aeruginosa PAK pilin suggests a main-chain-dominated mode of receptor binding.

Authors: B Hazes; P A Sastry; K Hayakawa; R J Read; R T Irvin
Journal: J Mol Biol Date: 2000-06-16 Impact factor: 5.469

6. Crystallographic analysis of the Pseudomonas aeruginosa strain K122-4 monomeric pilin reveals a conserved receptor-binding architecture.

Authors: Gerald F Audette; Randall T Irvin; Bart Hazes
Journal: Biochemistry Date: 2004-09-14 Impact factor: 3.162

7. The type IVB pili of Salmonella enterica serovar Typhi bind to the cystic fibrosis transmembrane conductance regulator.

Authors: Inez S M Tsui; Cecilia M C Yip; Jim Hackett; Christina Morris
Journal: Infect Immun Date: 2003-10 Impact factor: 3.441

8. Type IV pilin structure and assembly: X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin.

Authors: Lisa Craig; Ronald K Taylor; Michael E Pique; Brian D Adair; Andrew S Arvai; Mona Singh; Sarah J Lloyd; David S Shin; Elizabeth D Getzoff; Mark Yeager; Katrina T Forest; John A Tainer
Journal: Mol Cell Date: 2003-05 Impact factor: 17.970

Crystallization and preliminary X-ray diffraction analysis of Salmonella typhi PilS.

1. A HEX-1 crystal lattice required for Woronin body function in Neurospora crassa.

Review 2. Type IV pilus structure and bacterial pathogenicity.

3. Processing of X-ray diffraction data collected in oscillation mode.

4. Solvent content of protein crystals.

5. Crystal structure of Pseudomonas aeruginosa PAK pilin suggests a main-chain-dominated mode of receptor binding.

6. Crystallographic analysis of the Pseudomonas aeruginosa strain K122-4 monomeric pilin reveals a conserved receptor-binding architecture.

7. The type IVB pili of Salmonella enterica serovar Typhi bind to the cystic fibrosis transmembrane conductance regulator.

8. Type IV pilin structure and assembly: X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin.

9. NMR structure of a type IVb pilin from Salmonella typhi and its assembly into pilus.

10. Structure of the bundle-forming pilus from enteropathogenic Escherichia coli.

Review 1. Type IV pilin proteins: versatile molecular modules.

2. The physical basis of type 4 pilus-mediated microcolony formation by Vibrio cholerae O1.