Homotypic dimerization of a maltose kinase for molecular scaffolding

Scientific Reports

Volumn 4, Issue , 2014, Pages

  Li, Jun ^a   Guan, Xiaotao ^a   Shaw, Neil ^a,c   Chen, Weimin ^c   Dong, Yu ^a   Xu, Xiaoling ^c,d   Li, Xuemei ^a   Rao, Zihe ^a,b,c  

^a INSTITUTE OF BIOPHYSICS   (China)

^b TSINGHUA UNIVERSITY   (China)

^c NANKAI UNIVERSITY   (China)

^d HANGZHOU NORMAL UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE TRANSPORTER; MALTOSE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; BINDING SITE; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR GENETICS; MYCOBACTERIUM TUBERCULOSIS; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; MALTOSE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MONOSACCHARIDE TRANSPORT PROTEINS; MYCOBACTERIUM TUBERCULOSIS; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 84923045274     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep06418     Document Type: Article

References (36)

1. Iturriaga, G., Suarez, R. & Nova-Franco, B. Trehalose metabolism: from osmoprotection to signaling. Int J Mol Sci 10, 3793-3810 (2009).
2. De Smet, K. A.,Weston, A., Brown, I. N., Young, D. B. & Robertson, B. D. Three pathways for trehalose biosynthesis in mycobacteria. Microbiology 146 (Pt1), 199-208 (2000).
3. Elbein, A. D., Pan, Y. T., Pastuszak, I. & Carroll, D. New insights on trehalose: a multifunctional molecule. Glycobiology 13, 17R-27R (2003).
4. Winder, F. G., Tighe, J. J. & Brennan, P. J. Turnover of acylglucose, acyltrehalose and free trehalose during growth of Mycobacterium smegmatis on glucose. J Gen Microbiol 73, 539-546 (1972).
5. Mendes, V., Maranha, A., Alarico, S. & Empadinhas, N. Biosynthesis of mycobacterial methylglucose lipopolysaccharides. Nat Prod Rep 29, 834-844 (2012).
6. Sambou, T. et al. Capsular glucan and intracellular glycogen of Mycobacterium tuberculosis: biosynthesis and impact on the persistence in mice. Mol Microbiol 70, 762-774 (2008).
7. Roy, R. et al. Synthesis of alpha-Glucan in Mycobacteria Involves a Heterooctameric Complex of Trehalose Synthase TreS and Maltokinase Pep2. ACS Chem Biol 8, 2245-2255 (2013).
8. Kalscheuer, R. et al. Self-poisoning of Mycobacterium tuberculosis by targeting GlgE in an alpha-glucan pathway. Nat Chem Biol 6, 376-384 (2010).
9. Pan, Y. T. et al. Trehalose synthase converts glycogen to trehalose. FEBS J 275, 3408-3420 (2008).
10. Elbein, A. D., Pastuszak, I., Tackett, A. J., Wilson, T. & Pan, Y. T. Last step in the conversion of trehalose to glycogen: a mycobacterial enzyme that transfers maltose from maltose 1-phosphate to glycogen. J Biol Chem 285, 9803-9812 (2010).
11. Pal, K. et al. Crystal structure of full-length Mycobacterium tuberculosis H37Rv glycogen branching enzyme: insights of N-terminal beta-sandwich in substrate specificity and enzymatic activity. J Biol Chem 285, 20897-20903 (2010).
12. Sassetti, C. M., Boyd, D. H. Rubin, E. J. Genes required for mycobacterial growth defined by high density mutagenesis. Mol Microbiol 48, 77-84 (2003).
13. Griffin, J. E. et al. High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism. PLoS Pathog 7, e1002251 (2011).
14. Sani, M. et al. Direct visualization by cryo-EM of the mycobacterial capsular layer: a labile structure containing ESX-1-secreted proteins. PLoS Pathog 6, e1000794 (2010).
15. Niehues, B. et al. Isolation and characterization of maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes missouriensis. Arch Microbiol 180, 233-239 (2003).
16. Mendes, V., Maranha, A., Lamosa, P., da Costa, M. S. & Empadinhas, N. Biochemical characterization of the maltokinase from Mycobacterium bovis BCG. BMC Biochem 11, 21 (2010).
17. Caner, S. et al. The structure of the Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding mode. Glycobiology 23, 1075-1083 (2013).
18. Ravaud, S. et al. Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization. J Biol Chem 282, 28126-28136 (2007).
19. Taylor, S. S. & Kornev, A. P. Protein kinases: evolution of dynamic regulatory proteins. Trends Biochem Sci 36, 65-77 (2011).
20. Holm, L. Rosenstrom, P.Dali server: conservation mapping in 3D. Nucleic Acids Res 38, W545-549 (2010).
21. Ku, S. Y. et al. Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding. J Biol Chem 282, 22195-22206 (2007).
22. Peisach, D., Gee, P., Kent, C. & Xu, Z. The crystal structure of choline kinase reveals a eukaryotic protein kinase fold. Structure 11, 703-713 (2003).
23. Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J Mol Biol 372, 774-797 (2007).
24. Burk, D. L., Hon, W. C., Leung, A. K. & Berghuis, A. M. Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase. Biochemistry 40, 8756-8764 (2001).
25. Young, T. A., Delagoutte, B., Endrizzi, J. A., Falick, A. M. & Alber, T. Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases. Nat Struct Biol 10, 168-174 (2003).
26. Oliver, A. W. et al. Trans-activation of the DNA-damage signalling protein kinase Chk2 by T-loop exchange. EMBO J 25, 3179-3190 (2006).
27. Lassila, J. K., Zalatan, J. G. & Herschlag, D. Biological phosphoryl-transfer reactions: understanding mechanism and catalysis. Annu Rev Biochem 80, 669-702 (2011).
28. Bartek, J. & Lukas, J. DNA damage checkpoints: from initiation to recovery or adaptation. Curr Opin Cell Biol 19, 238-245 (2007).
29. Fukuda, K., Gupta, S., Chen, K., Wu, C. & Qin, J. The pseudoactive site of ILK is essential for its binding to alpha-Parvin and localization to focal adhesions. Mol Cell 36, 819-830 (2009).
30. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276, 307-326 (1997).
31. Schneider, T. R. & Sheldrick, G. M. Substructure solution with SHELXD. Acta Crystallogr D Biol Crystallogr 58, 1772-1779 (2002).
32. Echols, N. et al. Graphical tools for macromolecular crystallography in PHENIX. J Appl Crystallogr 45, 581-586 (2012).
33. Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60, 2126-2132 (2004).
34. McCoy, A. J. et al. Phaser crystallographic software. J Appl Crystallogr 40, 658-674 (2007).
35. Potterton, E., Briggs, P., Turkenburg, M. & Dodson, E. A graphical user interface to the CCP4 program suite. Acta Crystallogr D Biol Crystallogr 59, 1131-1137 (2003).
36. Shan, S. et al. Crystal structure of 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (IspE) from Mycobacterium tuberculosis. FASEB J 25, 1577-1584 (2011).