Structural basis of the sensor-synthase interaction in autoinduction of the quorum sensing signal DSF biosynthesis

Structure

Volumn 18, Issue 9, 2010, Pages 1199-1209

  Cheng, Zhihong ^a   He, Ya Wen ^a   Lim, Siew Choo ^a,b   Qamra, Rohini ^a   Walsh, Martin A ^c   Zhang, Lian Hui ^a,d   Song, Haiwei ^a,b,d  

^a INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Singapore)

^b NANYANG TECHNOLOGICAL UNIVERSITY   (Singapore)

^c EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

^d NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

COENZYME A; GLUTAMIC ACID; SYNTHETASE;

ARTICLE; CATALYSIS; CONFORMATION; ENZYME STRUCTURE; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; QUORUM SENSING;

BACTERIAL PROTEINS; CATALYTIC DOMAIN; ENOYL-COA HYDRATASE; MODELS, MOLECULAR; PROTEIN CONFORMATION; QUORUM SENSING; SIGNAL TRANSDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 77956300659     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2010.06.011     Document Type: Article

References (44)

1. Agnihotri G., Liu H.W. Enoyl-CoA hydratase. reaction, mechanism, and inhibition. Bioorg. Med. Chem. 2003, 11:9-20.
2. Bahnson B.J., Anderson V.E., Petsko G.A. Structural mechanism of enoyl-CoA hydratase: three atoms from a single water are added in either an E1cb stepwise or concerted fashion. Biochemistry 2002, 41:2621-2629.
3. Baikalov I., Schroder I., Kaczor-Grzeskowiak M., Grzeskowiak K., Gunsalus R.P., Dickerson R.E. Structure of the Escherichia coli response regulator NarL. Biochemistry 1996, 35:11053-11061.
4. Barber C.E., Tang J.L., Feng J.X., Pan M.Q., Wilson T.J., Slater H., Dow J.M., Williams P., Daniels M.J. A novel regulatory system required for pathogenicity of Xanthomonas campestris is mediated by a small diffusible signal molecule. Mol. Microbiol. 1997, 24:555-566.
5. Bassler B.L., Losick R. Bacterially speaking. Cell 2006, 125:237-246.
6. Bell A.F., Feng Y., Hofstein H.A., Parikh S., Wu J., Rudolph M.J., Kisker C., Whitty A., Tonge P.J. Stereoselectivity of enoyl-CoA hydratase results from preferential activation of one of two bound substrate conformers. Chem. Biol. 2002, 9:1247-1255.
7. Benning M.M., Haller T., Gerlt J.A., Holden H.M. New reactions in the crotonase superfamily: structure of methylmalonyl CoA decarboxylase from Escherichia coli. Biochemistry 2000, 39:4630-4639.
8. Boon C., Deng Y., Wang L.H., He Y., Xu J.L., Fan Y., Pan S.Q., Zhang L.H. A novel DSF-like signal from Burkholderia cenocepacia interferes with Candida albicans morphological transition. ISME J. 2008, 2:27-36.
9. Casino P., Rubio V., Marina A. Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction. Cell 2009, 139:325-336.
10. Colnaghi Simionato A.V., da Silva D.S., Lambais M.R., Carrilho E. Characterization of a putative Xylella fastidiosa diffusible signal factor by HRGC-EI-MS. J. Mass Spectrom. 2007, 42:490-496.
11. Djordjevic S., Stock A.M. Structural analysis of bacterial chemotaxis proteins: components of a dynamic signaling system. J. Struct. Biol. 1998, 124:189-200.
12. Dong Y.H., Wang L.Y., Zhang L.H. Quorum-quenching microbial infections: mechanisms and implications. Philos. Trans. R. Soc. Lond. B Biol. Sci. 2007, 362:1201-1211.
13. Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 2004, 60:2126-2132.
14. Engel C.K., Mathieu M., Zeelen J.P., Hiltunen J.K., Wierenga R.K. Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket. EMBO J. 1996, 15:5135-5145.
15. Engel C.K., Kiema T.R., Hiltunen J.K., Wierenga R.K. The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule. J. Mol. Biol. 1998, 275:847-859.
16. Feher V.A., Zapf J.W., Hoch J.A., Whiteley J.M., McIntosh L.P., Rance M., Skelton N.J., Dahlquist F.W., Cavanagh J. High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition. Biochemistry 1997, 36:10015-10025.
17. Fouhy Y., Scanlon K., Schouest K., Spillane C., Crossman L., Avison M.B., Ryan R.P., Dow J.M. Diffusible signal factor-dependent cell-cell signaling and virulence in the nosocomial pathogen Stenotrophomonas maltophilia. J. Bacteriol. 2007, 189:4964-4968.
18. Hamed R.B., Batchelar E.T., Clifton I.J., Schofield C.J. Mechanisms and structures of crotonase superfamily enzymes-how nature controls enolate and oxyanion reactivity. Cell. Mol. Life Sci. 2008, 65:2507-2527.
19. He Y.W., Zhang L.H. Quorum sensing and virulence regulation in Xanthomonas campestris. FEMS Microbiol. Rev. 2008, 32:842-857.
20. He Y.W., Wang C., Zhou L., Song H., Dow J.M., Zhang L.H. Dual signaling functions of the hybrid sensor kinase RpfC of Xanthomonas campestris involve either phosphorelay or receiver domain-protein interaction. J. Biol. Chem. 2006, 281:33414-33421.
21. He Y.W., Xu M., Lin K., Ng Y.J., Wen C.M., Wang L.H., Liu Z.D., Zhang H.B., Dong Y.H., Dow J.M., et al. Genome scale analysis of diffusible signal factor regulon in Xanthomonas campestris pv. campestris: identification of novel cell-cell communication-dependent genes and functions. Mol. Microbiol. 2006, 59:610-622.
22. Huang T.P., Wong A.C. A cyclic AMP receptor protein-regulated cell-cell communication system mediates expression of a FecA homologue in Stenotrophomonas maltophilia. Appl. Environ. Microbiol. 2007, 73:5034-5040.
23. Hubbard P.A., Yu W., Schulz H., Kim J.J. Domain swapping in the low-similarity isomerase/hydratase superfamily: the crystal structure of rat mitochondrial Delta3, Delta2-enoyl-CoA isomerase. Protein Sci. 2005, 14:1545-1555.
24. Kern D., Volkman B.F., Luginbuhl P., Nohaile M.J., Kustu S., Wemmer D.E. Structure of a transiently phosphorylated switch in bacterial signal transduction. Nature 1999, 402:894-898.
25. Kurimoto K., Fukai S., Nureki O., Muto Y., Yokoyama S. Crystal structure of human AUH protein, a single-stranded RNA binding homolog of enoyl-CoA hydratase. Structure 2001, 9:1253-1263.
26. Leslie, A.G.W. (1992). Joint CCP4 + ESF-EAMCB Newsletter on Protein Crystallography No. 26, 27-33.
27. McCoy A.J., Grosse-Kunstleve R.W., Adams P.D., Winn M.D., Storoni L.C., Read R.J. Phaser crystallographic software. J. Appl. Crystallogr. 2007, 40:658-674.
28. Milton D.L. Quorum sensing in vibrios: complexity for diversification. Int. J. Med. Microbiol. 2006, 296:61-71.
29. Mingarro I., Abad C., Braco L. Interfacial activation-based molecular bioimprinting of lipolytic enzymes. Proc. Natl. Acad. Sci. USA 1995, 92:3308-3312.
30. Morris R.J., Perrakis A., Lamzin V.S. ARP/wARP's model-building algorithms. I. The main chain. Acta Crystallogr. D Biol. Crystallogr. 2002, 58:968-975.
31. Muller-Newen G., Janssen U., Stoffel W. Enoyl-CoA hydratase and isomerase form a superfamily with a common active-site glutamate residue. Eur. J. Biochem. 1995, 228:68-73.
32. Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 1997, 53:240-255.
33. Mursula A.M., van Aalten D.M., Hiltunen J.K., Wierenga R.K. The crystal structure of delta(3)-delta(2)-enoyl-CoA isomerase. J. Mol. Biol. 2001, 309:845-853.
34. Partanen S.T., Novikov D.K., Popov A.N., Mursula A.M., Hiltunen J.K., Wierenga R.K. The 1.3 A crystal structure of human mitochondrial Delta3-Delta2-enoyl-CoA isomerase shows a novel mode of binding for the fatty acyl group. J. Mol. Biol. 2004, 342:1197-1208.
35. Potterton E., Briggs P., Turkenburg M., Dodson E. A graphical user interface to the CCP4 program suite. Acta Crystallogr. D Biol. Crystallogr. 2003, 59:1131-1137.
36. Sheldrick G.M. A short history of SHELX. Acta Crystallogr. A 2008, 64:112-122.
37. Slater H., Alvarez-Morales A., Barber C.E., Daniels M.J., Dow J.M. A two-component system involving an HD-GYP domain protein links cell-cell signalling to pathogenicity gene expression in Xanthomonas campestris. Mol. Microbiol. 2000, 38:986-1003.
38. Sola M., Gomis-Ruth F.X., Serrano L., Gonzalez A., Coll M. Three-dimensional crystal structure of the transcription factor PhoB receiver domain. J. Mol. Biol. 1999, 285:675-687.
39. Stock A.M., Mottonen J.M., Stock J.B., Schutt C.E. Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis. Nature 1989, 337:745-749.
40. Volkman B.F., Nohaile M.J., Amy N.K., Kustu S., Wemmer D.E. Three-dimensional solution structure of the N-terminal receiver domain of NTRC. Biochemistry 1995, 34:1413-1424.
41. Von Bodman S.B., Bauer W.D., Coplin D.L. Quorum sensing in plant-pathogenic bacteria. Annu. Rev. Phytopathol. 2003, 41:455-482.
42. Wang L.H., He Y., Gao Y., Wu J.E., Dong Y.H., He C., Wang S.X., Weng L.X., Xu J.L., Tay L., et al. A bacterial cell-cell communication signal with cross-kingdom structural analogues. Mol. Microbiol. 2004, 51:903-912.
43. Whitehead N.A., Barnard A.M., Slater H., Simpson N.J., Salmond G.P. Quorum-sensing in Gram-negative bacteria. FEMS Microbiol. Rev. 2001, 25:365-404.
44. Zhang L.H., Dong Y.H. Quorum sensing and signal interference: diverse implications. Mol. Microbiol. 2004, 53:1563-1571.