Crystal Structure of the Stationary Phase Survival Protein SurE with Metal Ion and AMP

Journal of Molecular Biology

Volumn 371, Issue 1, 2007, Pages 123-136

  Iwasaki, Wakana ^a   Miki, Kunio ^a,b  

^a Harima Institute ^*  (Japan)

^b KYOTO UNIVERSITY   (Japan)

Author keywords

crystal structure; phosphatase; quaternary structure; stationary phase survival protein; SurE

Indexed keywords

BACTERIAL PROTEIN; DIMER; MANGANESE; PROTEIN SURE; TETRAMER; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ASSAY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; THERMUS THERMOPHILUS; ULTRACENTRIFUGATION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA; THERMUS THERMOPHILUS;

EID: 34447107887     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.05.007     Document Type: Article

References (20)

1. Li C., Ichikawa J.K., Ravetto J.J., Kuo H.C., Fu J.C., and Clarke S. A new gene involved in stationary-phase survival located at 59 minutes on the Escherichia coli chromosome. J. Bacteriol. 176 (1994) 6015-6022
2. Li C., Wu P.Y., and Hsieh M. Growth-phase-dependent transcriptional regulation of the pcm and surE genes required for stationary-phase survival of Escherichia coli. Microbiology 143 (1997) 3513-3520
3. Visick J.E., Ichikawa J.K., and Clarke S. Mutations in the Escherichia coli surE gene increase isoaspartyl accumulation in a strain lacking the pcm repair methyltransferase but suppress stress-survival phenotypes. FEMS Microbiol. Letters 167 (1998) 19-25
4. Riehle M.M., Bennett A.F., and Long A.D. Genetic architecture of thermal adaptation in Escherichia coli. Proc. Natl Acad. Sci. USA 98 (2001) 525-530
5. Tréton B.Y., Le M., Dall T., and Gaillardin C.M. Complementation of Saccharomyces cerevisiae acid phosphatase mutation by a genomic sequence from the yeast Yarrowia lipolytica identifies a new phosphatase. Curr. Genet. 22 (1992) 345-355
6. Lee J.Y., Kwak J.E., Moon J., Eom S.H., Liong E.C., Pedelacq J.D., et al. Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family. Nature Struct. Biol. 8 (2001) 789-794
7. Zhang R.G., Skarina T., Katz J.E., Beasley S., Khachatryan A., Vyas S., et al. Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase. Structure 9 (2001) 1095-1106
8. Mura C., Katz J.E., Clarke S.G., and Eisenberg D. Structure and function of an archaeal homolog of survival protein E (SurEalpha): an acid phosphatase with purine nucleotide specificity. J. Mol. Biol. 326 (2003) 1559-1575
9. Proudfoot M., Kuznetsova E., Brown G., Rao N.N., Kitagawa M., Mori H., et al. General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG. J. Biol. Chem. 279 (2004) 54687-54694
10. Zhao R., Collins E.J., Bourret R.B., and Silversmith R.E. Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ. Nature Struct. Biol. 9 (2002) 570-575
11. Adachi S., Oguchi T., Tanida H., Park S.Y., Shimizu H., Miyatake H., et al. The RIKEN structural biology beamline II (BL44B2) at the SPring-8. Nuclear Instrum Methods Phy. Res. A 467-468 (2001) 711-714
12. Kumasaka T., Yamamoto M., Yamashita E., Moriyama H., and Ueki T. Trichromatic concept optimizes MAD experiments in synchrotron X-ray crystallography. Structure 10 (2002) 1205-1210
13. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
14. Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
15. Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallog. 30 (1997) 1022-1025
16. McRee D.E. XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
17. Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallog. sect. D 54 (1998) 905-921
18. Notredame C., Higgins D., and Heringa J. T-Coffee: a novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302 (2000) 205-217
19. Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24 (1991) 946-950
20. Merritt E.A., and Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277 (1997) 505-524