Crystal structure of the PSPTO-PSP protein from Pseudomonas syringae pv. tomato str. DC3000 in complex with d-glucose

Biochemical and Biophysical Research Communications

Volumn 397, Issue 1, 2010, Pages 82-86

  Zhang, Hong mei ^a   Gao, Yu ^a   Li, Mei ^a   Chang, Wen rui ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

Author keywords

Crystal structure; Glucose binding; PSP; YjgF

Indexed keywords

ARGININE; ASPARAGINE; GLUCOSE; GLUTAMIC ACID; GLYCINE; HYDROGEN; ISOLEUCINE; PERCHLORIC ACID SOLUBLE PROTEIN; PROLINE; RIBONUCLEASE; SERINE; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID COMPOSITION; ARTICLE; CELL METABOLISM; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME REGULATION; GENETIC CONSERVATION; GENETIC REGULATION; HYDROGEN BOND; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN QUATERNARY STRUCTURE; PSEUDOMONAS SYRINGAE; SEQUENCE HOMOLOGY;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; GLUCOSE; HEAT-SHOCK PROTEINS; HYDROGEN BONDING; PSEUDOMONAS SYRINGAE;

PSEUDOMONAS SYRINGAE PV. TOMATO;

EID: 77953610439     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.05.071     Document Type: Article

References (23)

1. Christopherson M.R., Schmitz G.E., and Downs D.M. YjgF is required for isoleucine biosynthesis when Salmonella enterica is grown on pyruvate medium. J. Bacteriol. 190 (2008) 3057-3062
2. Schmitz G., and Downs D.M. Reduced transaminase B (IlvE) activity caused by the lack of yjgF is dependent on the status of threonine deaminase (IlvA) in Salmonella enterica serovar Typhimurium. J. Bacteriol. 186 (2004) 803-810
3. Kim J.M., Yoshikawa H., and Shirahige K. A member of the YER057c/yjgf/Uk114 family links isoleucine biosynthesis and intact mitochondria maintenance in Saccharomyces cerevisiae. Genes Cells 6 (2001) 507-517
4. Oxelmark E., Marchini A., Malanchi I., Magherini F., Jaquet L., Hajibagheri M.A., Blight K.J., Jauniaux J.C., and Tommasino M. Mmf1p, a novel yeast mitochondrial protein conserved throughout evolution and involved in maintenance of the mitochondrial genome. Mol. Cell Biol. 20 (2000) 7784-7797
5. Oka T., Tsuji H., Noda C., Sakai K., Hong Y.M., Suzuki I., Munoz S., and Natori Y. Isolation and characterization of a novel perchloric acid-soluble protein inhibiting cell-free protein synthesis. J. Biol. Chem. 270 (1995) 30060-30067
6. Schmiedeknecht G., Kerkhoff C., Orso E., Stohr J., Aslanidis C., Nagy G.M., Knuechel R., and Schmitz G. Isolation and characterization of a 14.5-kDa trichloroacetic-acid-soluble translational inhibitor protein from human monocytes that is upregulated upon cellular differentiation. Eur. J. Biochem. 242 (1996) 339-351
7. Kanouchi H., Matsuo A., Oka T., Tachibana H., and Yamada K. Recombinant perchloric acid-soluble protein suppresses the immunoglobulin production of human-human hybridoma HB4C5 cells. In Vitro Cell. Dev. Biol. Anim. 39 (2003) 263-265
8. Kaneki K., Kanouchi H., Matsumoto M., Kawasaki Y., Akuzawa M., and Oka T. Down regulation of a novel protein, PSP, in rat hepatoma cdRLh 84-beared tumor. J. Vet. Med. Sci. 65 (2003) 781-785
9. Morishita R., Kawagoshi A., Sawasaki T., Madin K., Ogasawara T., Oka T., and Endo Y. Ribonuclease activity of rat liver perchloric acid-soluble protein, a potent inhibitor of protein synthesis. J. Biol. Chem. 274 (1999) 20688-20692
10. Levy-Favatier F., Leroux A., Antoine B., Nedelec B., and Delpech M. Upregulation of rat P23 (a member of the YjgF protein family) by fasting, glucose diet and fatty acid feeding. Cell. Mol. Life Sci. 61 (2004) 2886-2892
11. Kanouchi H., Miyamoto M., Oka T., Matsumoto M., Okamoto T., Tone S., and Minatogawa Y. Perchloric acid-soluble protein is expressed in enterocytes and goblet cells in the intestine and upregulated by dietary lipid. Biochim. Biophys. Acta 1760 (2006) 1380-1385
12. Sasagawa T., Oka T., Tokumura A., Nishimoto Y., Munoz S., Kuwahata M., Okita M., Tsuji H., and Natori Y. Analysis of the fatty acid components in a perchloric acid-soluble protein. Biochim. Biophys. Acta 1437 (1999) 317-324
13. Minor Z.O.a.W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 10
14. McCoy A.J. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D Biol. Crystallogr. 63 (2007) 32-41
15. Lamzin V.S., Perrakis A., and Wilson K.S. The ARP/wARP suite for automated construction and refinement of protein models. In: Rossmann M.G., and Arnold E. (Eds). International Tables for Crystallography. Volume F: Crystallography of Biological Macromolecules (2001), Dordrecht, Kluwer Academic Publishers, The Netherlands 720-722
16. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 2126-2132
17. Vagin A.A., Steiner R.A., Lebedev A.A., Potterton L., McNicholas S., Long F., and Murshudov G.N. REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 2184-2195
18. Laskowski M.W.M.R.A., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures export. J. Appl. Cryst. 26 (1993) 9
19. Mistiniene E., Pozdniakovaite N., Popendikyte V., and Naktinis V. Structure-based ligand binding sites of protein p14.5, a member of protein family YER057c/YIL051c/YjgF. Int. J. Biol. Macromol. 37 (2005) 61-68
20. Burman J.D., Stevenson C.E., Sawers R.G., and Lawson D.M. The crystal structure of Escherichia coli TdcF, a member of the highly conserved YjgF/YER057c/UK114 family. BMC Struct. Biol. 7 (2007) 30
21. Manjasetty B.A., Delbruck H., Pham D.T., Mueller U., Fieber-Erdmann M., Scheich C., Sievert V., Bussow K., Niesen F.H., Weihofen W., Loll B., Saenger W., and Heinemann U. Crystal structure of Homo sapiens protein hp14.5. Proteins 54 (2004) 797-800
22. Kanouchi H., Oka T., Asagi K., Tachibana H., and Yamada K. Expression and cellular distribution of perchloric acid-soluble protein is dependent on the cell-proliferating states of NRK-52E cells. Cell. Mol. Life Sci. 57 (2000) 1103-1108
23. Kanouchi H., Matsumoto M., Taga M., Yamada K., Oka T., Tone S., and Minatogawa Y. Nuclear transfer of perchloric acid-soluble protein by endoplasmic reticulum stressors. Protein Sci. 14 (2005) 2344-2349