Crystal structures of mycobacterium tuberculosis GlgE and complexes with non-covalent inhibitors

Scientific Reports

Volumn 5, Issue , 2015, Pages

  Lindenberger, Jared J ^a   Kumar Veleti, Sri ^a   Wilson, Brittney N ^a   Sucheck, Steven J ^a   Ronning, Donald R ^a  

^a UNIVERSITY OF TOLEDO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; ENZYME INHIBITOR; GLUCOSYLTRANSFERASE; MALTOSYLTRANSFERASE;

ANTAGONISTS AND INHIBITORS; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; MYCOBACTERIUM TUBERCULOSIS; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; GLUCOSYLTRANSFERASES; MYCOBACTERIUM TUBERCULOSIS;

EID: 84938824086     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep12830     Document Type: Article

References (33)

1. WHO. Global tuberculosis report 2014. World Health Organization, (2014).
2. Ford, C. B. et al. Use of whole genome sequencing to estimate the mutation rate of Mycobacterium tuberculosis during latent infection. Nature genetics 43, 482-486 (2011).
3. Moonan, P. K. et al. Does directly observed therapy (DOT) reduce drug resistant tuberculosis? Bmc Public Health 11, 19 (2011).
4. Udwadia, Z. F., Amale, R. A., Ajbani, K. K. & Rodrigues, C. Totally drug-resistant tuberculosis in India. Clinical infectious diseases: an official publication of the Infectious Diseases Society of America 54, 579-581 (2012).
5. Kalscheuer, R. et al. Self-poisoning of Mycobacterium tuberculosis by targeting GlgE in an alpha-glucan pathway. Nature chemical biology 6, 376-384 (2010).
6. Chandra, G., Chater, K. F. & Bornemann, S. Unexpected and widespread connections between bacterial glycogen and trehalose metabolism. Microbiology 157, 1565-1572 (2011).
7. Syson, K. et al. Structure of Streptomyces maltosyltransferase GlgE, a homologue of a genetically validated anti-tuberculosis target. The Journal of biological chemistry 286, 38298-38310 (2011).
8. Syson, K. et al. Structural insight into how Streptomyces coelicolor maltosyl transferase GlgE binds alpha-maltose 1-phosphate and forms a maltosyl-enzyme intermediate. Biochemistry 53, 2494-2504 (2014).
9. Davies, GJ, Wilson, KS & Henrissat, B. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem J 321, 557-559 (1997).
10. Veleti, S. K., Lindenberger, J. J., Thanna, S., Ronning, D. R. & Sucheck, S. J. Synthesis of a poly-hydroxypyrolidine-based inhibitor of Mycobacterium tuberculosis GlgE. J Org Chem 79, 9444-9450 (2014).
11. Schirmer, T., Keller, T. A., Wang, Y. F. & Rosenbusch, J. P. Structural Basis for Sugar Translocation through Maltoporin Channels at 3.1-Angstrom Resolution. Science 267, 512-514 (1995).
12. Popov, D. et al. Crystal Structure of A-Amylose: A Revisit from Synchrotron Microdiffraction Analysis of Single Crystals. Macromolecules 42, 1167-1174 (2009).
13. Wimmerova, M. et al. Stacking interactions between carbohydrate and protein quantified by combination of theoretical and experimental methods. PloS one 7, e46032 (2012).
14. Patil, R. et al. Optimized hydrophobic interactions and hydrogen bonding at the target-ligand interface leads the pathways of drug-designing. PloS one 5, e12029 (2010).
15. Sarkar, A. & Kellogg, G. E. Hydrophobicity-shake flasks, protein folding and drug discovery. Current topics in medicinal chemistry 10, 67-83 (2010).
16. Veleti, S. K., Lindenberger, J. J., Ronning, D. R. & Sucheck, S. J. Synthesis of a C-phosphonate mimic of maltose-1-phosphate and inhibition studies on Mycobacterium tuberculosis GlgE. Bioorg Med Chem 22, 1404-1411 (2014).
17. Lillelund, V. H., Jensen, H. H., Liang, X. F. & Bols, M. Recent developments of transition-state analogue glycosidase inhibitors of non-natural product origin. Chem Rev 102, 515-553 (2002).
18. Schramm, V. L. Transition States, analogues, and drug development. ACS chemical biology 8, 71-81 (2013).
19. Gloster, T. M. & Davies, G. J. Glycosidase inhibition: assessing mimicry of the transition state. Organic & biomolecular chemistry 8, 305-320 (2010).
20. Unrau, P. J. & Bartel, D. P. An oxocarbenium-ion intermediate of a ribozyme reaction indicated by kinetic isotope effects. Proceedings of the National Academy of Sciences of the United States of America 100, 15393-15397 (2003).
21. Provencher, L., Steensma, D. H. & Wong, C. H. Five-membered ring azasugars as potent inhibitors of alpha-L-rhamnosidase (naringinase) from Penicillium decumbens. Bioorg Med Chem 2, 1179-1188 (1994).
22. Borges de Melo, E., da Silveira, G. & Carvalho, I. alpha-And beta-Glucosidase inhibitors: chemical structure and biological activity. Tetrahedron 62, 10277-10302 (2006).
23. Wells, J. A. & McClendon, C. L. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 450, 1001-1009 (2007).
24. Branson, T. R. & Turnbull, W. B. Bacterial toxin inhibitors based on multivalent scaffolds. Chemical Society reviews 42, 4613-4622 (2013).
25. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol 276, 307-326 (1997).
26. Afonine, P. V. et al. Towards automated crystallographic structure refinement with phenix.refine. Acta crystallographica Section D, Biological crystallography 68, 352-367 (2012).
27. McCoy, A. J. et al. Phaser crystallographic software. Journal of applied crystallography 40, 658-674 (2007).
28. Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta crystallographica Section D, Biological crystallography 66, 213-221 (2010).
29. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta crystallographica Section D, Biological crystallography 66, 486-501 (2010).
30. Moriarty, N. W., Grosse-Kunstleve, R. W. & Adams, P. D. electronic Ligand Builder and Optimization Workbench (eLBOW): a tool for ligand coordinate and restraint generation. Acta crystallographica Section D, Biological crystallography 65, 1074-1080 (2009).
31. Chen, V. B. et al. MolProbity: all-Atom structure validation for macromolecular crystallography. Acta crystallographica Section D, Biological crystallography 66, 12-21 (2010).
32. Robert, X. & Gouet, P. Deciphering key features in protein structures with the new ENDscript server. Nucleic acids research 42, W320-324 (2014).
33. Thanna, S., Lindenberger, J. J., Gaitonde, V. V., Ronning, D. R. & Sucheck, S. J. Synthesis of 2-deoxy-2,2-difluoro-?-maltosyl fluoride and its X-ray structure in complex with Streptomyces coelicolor GlgEI-V279S. Org Biomol Chem 13 (27): 7542-50 (2015).