Identification and characterization of the lipid-binding property of GrlR, a locus of enterocyte effacement regulator

Biochemical Journal

Volumn 420, Issue 2, 2009, Pages 191-199

  Jobichen, Chacko ^a   Fernandis, Aaron Z ^b   Velazquez Campoy, Adrian ^c   Leung, Ka Yin ^a,d   Mok, Yu Keung ^a   Wenk, Markus R ^a,b   Sivaraman, J ^a  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^b NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^c UNIVERSITY OF ZARAGOZA   (Spain)

^d TRINITY WESTERN UNIVERSITY   (Canada)

Author keywords

barrel protein; Global regulator of LEE (locus of enterocyte effacement) repressor (Gr1R); Lipid; Lipocalin; Type III secretion system (T3SS)

Indexed keywords

C-TERMINUS; ELECTROSPRAY; GLOBAL REGULATOR OF LEE (LOCUS OF ENTEROCYTE EFFACEMENT) REPRESSOR (GR1R); GRAM-NEGATIVE BACTERIA; HYDROPHOBIC CAVITIES; ISOTHERMAL TITRATION CALORIMETRY; LACTOGLOBULIN; LIPID BINDING; LIPID SPECIES; LIPID-BINDING PROTEINS; LIPOCALIN; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLGLYCEROL; STRUCTURE-BASED; TYPE III SECRETION SYSTEM (T3SS);

BACTERIA; ELECTROSPRAY IONIZATION; HYDROPHOBICITY; PROTEINS;

BINDING ENERGY;

BETA LACTOGLOBULIN; GLOBAL REGULATOR OF LOCUS OF ENTEROCYTE EFFACEMENT REPRESSOR PROTEIN; LIPID BINDING PROTEIN; LIPOCALIN; LYSOPHOSPHATIDIC ACID; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLGLYCEROL; PROTEIN GRLR; REGULATOR PROTEIN; REPRESSOR PROTEIN; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; GRLR PROTEIN, E COLI; LEE PROTEIN, E COLI; PHOSPHOPROTEIN;

ARTICLE; CONTROLLED STUDY; ELECTROSPRAY; HYDROPHOBICITY; INTESTINE CELL; ISOTHERMAL TITRATION CALORIMETRY; LIPID ANALYSIS; LIPOPHILICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN LIPID INTERACTION; PROTEIN STRUCTURE; STRUCTURAL HOMOLOGY; STRUCTURE ACTIVITY RELATION; TYPE III SECRETION SYSTEM; AMINO ACID SEQUENCE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

EUKARYOTA; NEGIBACTERIA;

AMINO ACID SEQUENCE; BINDING SITES; ESCHERICHIA COLI PROTEINS; HYDROPHOBICITY; LIPOCALINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHATIDYLETHANOLAMINES; PHOSPHATIDYLGLYCEROLS; PHOSPHOPROTEINS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; REPRESSOR PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 66549126907     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20081588     Document Type: Article

References (32)

1. Jobichen, C., Li, M., Yerushalmi, G., Tan, Y., Mok, Y., Rosenshine, I., Leung, K. and Sivaraman, J. (2007) Structure of GrlR and the implication of its EDED motif in mediating the regulation of type III secretion system in EHEC. PLoS Pathog. 3, e69
2. Bishop, R., Penfold, S., Frost, L., Höltje, J. and Weiner, J. (1995) Stationary phase expression of a novel Escherichia coli outer membrane lipoprotein and its relationship with mammalian apolipoprotein D. Implications for the origin of lipocalins. J. Biol. Chem. 270, 23097-23103
3. Bishop, R. (2000) The bacterial lipocalins. Biochim. Biophys. Acta. 1482, 73-83
4. Akerstrom, B., Flower, D. and Salier, J. (2000) Lipocalins: unity in diversity. Biochim. Biophys. Acta 1482, 1-8
5. Flower, D., North, A. and Sansom, C. (2000) The lipocalin protein family: structural and sequence overview. Biochim. Biophys. Acta 1482, 9-24
6. Flower, D. (2000) Experimentally determined lipocalin structures. Biochim. Biophys. Acta 1482, 46-56
7. Grzyb, J., Latowski, D. and Strzalka, K. (2006) Lipocalins - a family portrait. J. Plant Physiol. 163, 895-915
8. Flower, D. (1995) Multiple molecular recognition properties of the lipocalin protein family. J. Mol. Recognit. 8, 185-195
9. Flower, D., North, A. and Attwood, T. (1993) Structure and sequence relationships in the lipocalins and related proteins. Protein Sci. 2, 753-761
10. Campanacci, V., Nurizzo, D., Spinelli, S., Valencia, C., Tegoni, M. and Cambillau, C. (2004) The crystal structure of the Escherichia coli lipocalin Blc suggests a possible role in phospholipid binding. FEBS Lett. 562, 183-188
11. Flower, D. (1995) The up-and-down β-barrel proteins: three of a kind. FASEB J. 9, 566-567
12. Matthews, B. (1968) Solvent content of protein crystals. J. Mol. Biol. 33, 491-497
13. Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
14. McCoy, A. (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr., Sect. D: Biol. Crystallogr. 63, 32-41
15. CCP4 (Collaborative Computational Project, number 4) (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50, 760-763
16. Brünger, A., Adams, P., Clore, G., DeLano, W., Gros, P., Grosse-Kunstleve, R., Jiang, J., Kuszewski, J., Nilges, M., Pannu, N. et al. (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr., Sect. D: Biol. Crystallogr. 54, 905-921
17. Jones, T., Zou, J., Cowan, S. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr., Sect. A: Found. Crystallogr. 47, 110-119
18. Laskowski, R., Moss, D. and Thornton, J. (1993) Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231, 1049-1067
19. Holm, L. and Sander, C. (1996) Mapping the protein universe. Science 273, 595-603
20. Altschul, S., Madden, T., Schäffer, A., Zhang, J., Zhang, Z., Miller, W. and Lipman, D. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402
21. Lario, P., Pfuetzner, R., Frey, E., Creagh, L., Haynes, C., Maurelli, A. and Strynadka, N. (2005) Structure and biochemical analysis of a secretin pilot protein. EMBO J. 24, 1111-1121
22. Wyman, J. and Gill, S. (1990) Binding and Linkage, Functional Chemistry of Biological Macromolecules, University Science Books, Mill Valley, CA
23. Hwang, P., Choy, W., Lo, E., Chen, L., Forman-Kay, J., Raetz, C., Privé, G., Bishop, R. and Kay, L. (2002) Solution structure and dynamics of the outer membrane enzyme PagP by NMR. Proc. Natl. Acad. Sci. U.S.A. 99, 13560-13565
24. Dowhan, W. (1997) Molecular basis for membrane phospholipid diversity: why are there so many lipids? Annu. Rev. Biochem. 66, 199-232
25. Böcskei, Z., Groom, C., Flower, D., Wright, C., Phillips, S., Cavaggioni, A., Findlay, J. and North, A. (1992) Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography. Nature 360, 186-188
26. Cavaggioni, A., Findlay, J. and Tirindelli, R. (1990) Ligand binding characteristics of homologous rat and mouse urinary proteins and pyrazine-binding protein of calf. Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol. 96, 513-520
27. Monaco, H. and Zanotti, G. (1992) Three-dimensional structure and active site of three hydrophobic molecule-binding proteins with significant amino acid sequence similarity. Biopolymers 32, 457-465
28. Wu, S. Y., Perez, M. D., Puyol, P. and Sawyer, L. (1999) β-Lactoglobulin binds palmitate within its central cavity. J. Biol. Chem. 274, 170-174
29. Qin, B. Y., Creamer, L. K., Baker, E. N. and Jameson, G. B. (1998) 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin. FEBS Lett. 438, 272-278
30. Kontopidis, G., Holt, C. and Sawyer, L. (2002) The ligand-binding site of bovine β-lactoglobulin: evidence for a function? J. Mol. Biol. 318, 1043-1055
31. Larkin, M., Blackshields, G., Brown, N., Chenna, R., McGettigan, P., McWilliam, H., Valentin, F., Wallace, I., Wilm, A., Lopez, R. et al. (2007) Clustal W and Clustal X version 2.0. Bioinformatics 23, 2947-2948
32. Gouet, P., Courcelle, E., Stuart, D. and Métoz, F. (1999) ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15, 305-308