Structure of catalase HPII from Escherichia coli at 1.9 Å Resolution

Proteins: Structure, Function and Genetics

Volumn 34, Issue 2, 1999, Pages 155-166

  Bravo, Jerónimo ^a   Mate, Maria J ^a   Schneider, Thomas ^b   Switala, Jack ^c   Wilson, Keith ^b,d   Loewen, Peter C ^c   Fita, Ignacio ^a  

^a DEPT OF ENVIRONMENTAL CHEMISTRY   (Spain)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^c UNIVERSITY OF MANITOBA   (Canada)

^d UNIVERSITY OF YORK   (United Kingdom)

Author keywords

Bacterial catalase; Channels; Cryocrystallography; Flavodoxin domain; Heme d

Indexed keywords

CATALASE; CATALASE HPII; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME PURIFICATION; ENZYME STRUCTURE; ESCHERICHIA COLI; HYDROPHILICITY; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CATALASE; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HEME; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NADP; PROTEIN CONFORMATION; WATER;

BACTERIA (MICROORGANISMS); BOVINAE; ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0033081072     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19990201)34:2<155::AID-PROT1>3.0.CO;2-P     Document Type: Article

References (33)

1. Murthy MRN, Reid TJ, Sicignano A, Tanaka N, Rossmann, M. Structure of beef liver catalase. J Mol Biol 1981;152:465-499.
2. Fita I, Silva AM, Murthy MRN, Rossmann MG. The refined structure of beef liver catalase at 2.5 Å resolution. Acta Crystallogr B 1986;42:497-515.
3. Vainshtein BK, Melik-Adamyan WR, Barynin VV, Vagin AA, Grebenko AI. Three-dimensional structure of the enzyme catalase. Nature 1981;293:411-412.
4. Vainshtein BK, Melik-Adamyan WR, Barynin VV, et al. Three-dimensional structure of catalase from Penicillium vitale at 2.0 Å resolution. J Mol Biol 1986;188:49-61.
5. Berthet S, Nykyri LM, Bravo J, et al. Crystallization and preliminary structural analysis of catalase A from Saccharomyces cerevisiae. Protein Sci. 1997;6:481-483.
6. Murshudov GN, Melik-Adamyan WR, Grebenko AI, et al. Three-dimensional structure of catalase from Micrococcus lysodeikticus at 1.5 Å resolution. FEBS Letts 1992;312:127-131.
7. Gouet P, Jouve HM, Dideberg O. Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH. J Mol Biol 1995;249:933-954.
8. Bravo J, Verdaguer N, Tormo J, Betzel C, Switala J, Loewen PC, Fita I. Crystal structure of catalase HPII from Escherichia coli. Structure 1995;3:491-502.
9. Loewen PC, Switala J, von Ossowski I, et al. Catalase HPII of Escherichia coli catalyzes the conversion of protoheme to cis-heme d. Biochemistry 1993;32:10159-10164.
10. Murshudov GN, Grebenko AI, Barynin V, et al. Structure of the heme d of Penicillium vitale and Escherichia coli catalases. J Biol Chem 1996;271:8863-8868.
11. Bravo J, Fita I, Ferrer JC, et al. Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli. Protein Sci. 1997;6:1016-1023.
12. Mulvey MR, Sorby PA, Triggs-Raine BL, Loewen PC. Cloning and physical characterization of katE and katF required for catalase HPII expression in Escherichia coli. Gene 1988;73:337-345.
13. Von Ossowski I, Mulvey MR, Leco PA, Borys A, Loewen PC. Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII. J Bacteriol 1991;173:514-520.
14. Loewen PC, Switala J. Purification and characterization of catalase HPII from Escherichia coli. K12. Biochem. Cell Biol 1986;64: 638-646.
15. Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Meth. Enzymol 1996;276:307-326.
16. Brünger AT. XPLOR Manual.Version 3. New Haven, CT: Yale University; 1992. 405 p.
17. Roussel A, Cambillau C. TURBO-FRODO, Manual. Mountain View, CA: Silicon Graphics Directory, Silicon Graphics; 1993. 170 p.
18. Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps. Acta Crystallogr. 1990;47:110-119.
19. Kleywegt GJ, Jones TA. Detection, delineation, measurement and display of molecules. Acta Crystallogr D 1994;50:178-185.
20. Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Crystallogr 1993;26:283-291.
21. Melik-Adamyan WR, Barynin VV, Vagin AA, et al. Comparison of beef liver and Penicillium vitale catalases. J Mol Biol 1936;188: 63-72.
22. Sevinc S, Ens W, Loewen PC. The cysteines of catalase HPII of Escherichia coli, including Cys438 which is blocked, do not have a catalytic role. Eur J Biochem 1995;230:127-132.
23. Jouve HM, Tessier S, Pelmont J. Purification and properties of the Proteus mirabilis catalase. Can J Biochem Cell Biol 1983;61:8-14.
24. Nichols A, Bharadwaj R, Honig B. GRASP-Graphical representation and analysis of surface properties. Biophys J 1993;64:A116.
25. Bergdoll M, Remy M-H, Cagon C, Masson J-M, Dumas P. Proline-dependent oligomerization with arm exchange. Structure 1997;5: 391-401.
26. Sevinc MS, Switala J, Bravo J, Fita I, Loewen PC. Truncation and heme pocket mutations reduce production of functional catalase HPII in Escherichia coli. Protein Eng. 1998;11:549-555.
27. Fita I, Rossmann MG. The active center of catalase. J Mol Biol 1985;185:21-37.
28. Hillar A, Nicholls P, Switala J, Loewen PC. NADPH binding and control of catalase compound II formation: Comparison of bovine, yeast, and Escherichia coli enzymes. Biochem J 1994;300:531-539.
29. Fita I, Rossmann MG. The NADPH binding site on beef liver catalase. Proc. Natl. Acad. Sci. USA 1985;82:1604-1608.
30. Kirkman HN, Gaetani GF. Catalase: a tetrameric enzyme with four tightly bound molecules of NADPH. Proc. Natl. Acad. Sci. USA. 1984;81:4343-4347.
31. Schonbaum GR, Chance B. Catalase. In: Boyer PD, editor. The enzymes, Vol 13. New York: Academic Press; 1976. p 363-408.
32. Chiu JT, Loewen PC, Switala J, Gennis RB, Timkovich R. Proposed structure for the prosthetic group of the catalase HPII from Escherichia coli. J Am Chem Soc 1989;111:7046-7050.
33. Bravo J, Fita I, Gouet P, Jouve HM, Melik-Adamyan W, Murshudov GN. Structure of catalases. In: Scandalios JG, editor. Oxidative stress and the molecular biology of antioxidant defenses. Cold Spring Harbor, NT: Cold Spring Harbor Laboratory Press; 1997. p 407-445.