دورية أكاديمية
أعرض في EDS

Induced conformational changes in the activation of the Pseudomonas aeruginosa type III toxin, ExoU.

التفاصيل البيبلوغرافية
العنوان: Induced conformational changes in the activation of the Pseudomonas aeruginosa type III toxin, ExoU.
المؤلفون: Benson MA; Center for Infectious Disease Research, Department of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, Wisconsin, USA., Komas SM, Schmalzer KM, Casey MS, Frank DW, Feix JB
المصدر: Biophysical journal [Biophys J] 2011 Mar 02; Vol. 100 (5), pp. 1335-43.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural
اللغة: English
بيانات الدورية: Publisher: Cell Press Country of Publication: United States NLM ID: 0370626 Publication Model: Print Cited Medium: Internet ISSN: 1542-0086 (Electronic) Linking ISSN: 00063495 NLM ISO Abbreviation: Biophys J Subsets: MEDLINE
أسماء مطبوعة: Publication: Cambridge, MA : Cell Press
Original Publication: New York, Published by Rockefeller University Press [etc.] for the Biophysical Society.
مواضيع طبية MeSH: Pseudomonas aeruginosa*, Bacterial Proteins/*chemistry , Bacterial Proteins/*metabolism , Catalytic Domain/*drug effects, Animals ; Cattle ; Electron Spin Resonance Spectroscopy ; Spin Labels ; Superoxide Dismutase/pharmacology ; Superoxide Dismutase-1
مستخلص: ExoU is a 74-kDa, water-soluble toxin injected directly into mammalian cells through the type III secretion system of the opportunistic pathogen, Pseudomonas aeruginosa. Previous studies have shown that ExoU is a Ca(2+)-independent phospholipase that requires a eukaryotic protein cofactor. One protein capable of activating ExoU and serving as a required cofactor was identified by biochemical and proteomic methods as superoxide dismutase (SOD1). In these studies, we carried out site-directed spin-labeling electron paramagnetic resonance spectroscopy to examine the effects of SOD1 and substrate liposomes on the structure and dynamics of ExoU. Local conformational changes within the catalytic site were observed in the presence of substrate liposomes, and were enhanced by the addition of SOD1 in a concentration-dependent manner. Conformational changes in the C-terminal domain of ExoU were observed upon addition of cofactor, even in the absence of liposomes. Double electron-electron resonance experiments indicated that ExoU samples multiple conformations in the resting state. In contrast, addition of SOD1 induced ExoU to adopt a single, well-defined conformation. These studies provide, to our knowledge, the first direct evidence for cofactor- and membrane-induced conformational changes in the mechanism of activation of ExoU.
(Copyright © 2011 Biophysical Society. Published by Elsevier Inc. All rights reserved.)
References: Biochemistry. 2006 Aug 29;45(34):10368-75. (PMID: 16922513)
Science. 1999 May 21;284(5418):1322-8. (PMID: 10334981)
Clin Chim Acta. 2010 Feb;411(3-4):190-7. (PMID: 19900431)
Infect Immun. 2006 May;74(5):2552-61. (PMID: 16622190)
Diagn Microbiol Infect Dis. 2009 Jul;64(3):311-9. (PMID: 19345039)
Infect Immun. 2010 Aug;78(8):3346-57. (PMID: 20479080)
Cell Microbiol. 2006 Aug;8(8):1294-309. (PMID: 16882033)
Biochemistry. 2007 Sep 11;46(36):10248-57. (PMID: 17696498)
Clin Infect Dis. 2004 Aug 1;39(3):309-17. (PMID: 15306996)
Protein Sci. 2009 Aug;18(8):1637-52. (PMID: 19585559)
Burns. 2001 Mar;27(2):129-30. (PMID: 11226648)
J Bacteriol. 2005 Feb;187(3):1192-5. (PMID: 15659695)
Proc Natl Acad Sci U S A. 2008 Dec 16;105(50):19666-71. (PMID: 19066219)
Biochemistry. 1989 Sep 19;28(19):7806-12. (PMID: 2558712)
Biochemistry. 2008 Dec 30;47(52):13878-86. (PMID: 19053284)
Biochemistry. 2006 Sep 12;45(36):10847-54. (PMID: 16953570)
J Biol Chem. 2003 Oct 17;278(42):41326-32. (PMID: 12915403)
Science. 2004 Oct 15;306(5695):491-5. (PMID: 15486302)
Biochemistry. 2002 Feb 5;41(5):1464-73. (PMID: 11814339)
Nat Rev Microbiol. 2009 Sep;7(9):654-65. (PMID: 19680249)
Methods Enzymol. 2007;423:52-116. (PMID: 17609127)
J Infect Dis. 2001 Jun 15;183(12):1767-74. (PMID: 11372029)
Infect Immun. 2001 Sep;69(9):5908-10. (PMID: 11500471)
J Trauma. 2007 Jul;63(1):164-71. (PMID: 17622885)
Trends Biochem Sci. 2002 Jun;27(6):288-95. (PMID: 12069788)
Curr Opin Struct Biol. 2006 Oct;16(5):644-53. (PMID: 16949813)
Curr Opin Microbiol. 2002 Feb;5(1):81-6. (PMID: 11834374)
Biochemistry. 2003 Nov 18;42(45):13106-12. (PMID: 14609320)
Clin Microbiol Rev. 2002 Apr;15(2):194-222. (PMID: 11932230)
Nature. 2006 Nov 30;444(7119):567-73. (PMID: 17136086)
J Bacteriol. 2010 Apr;192(7):1801-12. (PMID: 20097856)
Biochemistry. 2001 Apr 3;40(13):3828-46. (PMID: 11300763)
J Magn Reson. 2000 Feb;142(2):331-40. (PMID: 10648151)
Proc Natl Acad Sci U S A. 2008 May 27;105(21):7439-44. (PMID: 18490656)
Crit Care Med. 2002 Mar;30(3):521-8. (PMID: 11990909)
EMBO J. 2003 Jun 16;22(12):2959-69. (PMID: 12805211)
J Bacteriol. 2001 Jul;183(14):4330-44. (PMID: 11418575)
Mol Microbiol. 1997 Aug;25(3):547-57. (PMID: 9302017)
Biophys J. 2006 Apr 15;90(8):2922-9. (PMID: 16443663)
J Mol Biol. 2009 Oct 30;393(3):586-97. (PMID: 19715702)
Infect Immun. 2005 Jan;73(1):573-82. (PMID: 15618197)
Methods Cell Biol. 2008;84:617-58. (PMID: 17964945)
Biochemistry. 2009 Sep 22;48(37):8765-7. (PMID: 19691291)
Biochemistry. 2006 May 2;45(17):5538-50. (PMID: 16634635)
Nat Struct Biol. 2000 Sep;7(9):735-9. (PMID: 10966640)
معلومات مُعتمدة: P41 EB001980 United States EB NIBIB NIH HHS; R01 AI049577 United States AI NIAID NIH HHS; EB001980 United States EB NIBIB NIH HHS; AI49577 United States AI NIAID NIH HHS
المشرفين على المادة: 0 (Bacterial Proteins)
0 (Spin Labels)
0 (pseudomonas exoprotein A protein, Pseudomonas aeruginosa)
EC 1.15.1.1 (Superoxide Dismutase)
EC 1.15.1.1 (Superoxide Dismutase-1)
تواريخ الأحداث: Date Created: 20110301 Date Completed: 20110602 Latest Revision: 20211020
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC3043214
DOI: 10.1016/j.bpj.2011.01.056
PMID: 21354407
قاعدة البيانات: MEDLINE
الوصف
تدمد:1542-0086
DOI:10.1016/j.bpj.2011.01.056