Rv3389C from Mycobacterium tuberculosis, a member of the (R)-specific hydratase/dehydratase family

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1774, Issue 2, 2007, Pages 303-311

  Sacco, Emmanuelle ^a   Legendre, Virginie ^a   Laval, Françoise ^a   Zerbib, Didier ^a   Montrozier, Henri ^a   Eynard, Nathalie ^a   Guilhot, Christophe ^a   Daffé, Mamadou ^a   Quémard, Annaïk ^a  

^a INSTITUT DE PHARMACOLOGIE ET DE BIOLOGIE STRUCTURALE   (France)

Author keywords

(R) specific 3 hydroxyacyl dehydratase; Double hot dog fold; Enoyl CoA hydratase; Fatty acid biosynthesis; Hydratase 2; Mycobacterium

Indexed keywords

ACYL CARRIER PROTEIN; ENOYL COENZYME A HYDRATASE; FATTY ACID; FATTY ACID SYNTHASE; FATTY ACID SYNTHASE TYPE II; HYDROLYASE; MUTANT PROTEIN; MYCOLIC ACID; RECOMBINANT PROTEIN; RV3389C PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BIOINFORMATICS; BIOSYNTHESIS; CATALYSIS; ENZYME ANALYSIS; ENZYME SUBSTRATE; FATTY ACID ANALYSIS; HYDRATION; MYCOBACTERIUM TUBERCULOSIS; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN PURIFICATION;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CATALYSIS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM TUBERCULOSIS; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

CANIS FAMILIARIS; CORYNEBACTERINEAE; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS;

EID: 33846833567     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.11.016     Document Type: Article

References (45)

1. Daffé M., and Draper P. The envelope layers of mycobacteria with reference to their pathogenicity. Adv. Microb. Physiol. 39 (1998) 131-203
2. Alvarez H.M., Mayer F., Fabritius D., and Steinbüchel A. Formation of intracytoplasmic lipid inclusions by Rhodococcus opacus strain PD630. Arch. Microbiol. 165 (1996) 377-386
3. Marrakchi H., Lanéelle G., and Quémard A. InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II. Microbiology 146 (2000) 289-296
4. Marrakchi H., Ducasse S., Labesse G., Montrozier H., Margeat E., Emorine L., Charpentier X., Daffé M., and Quémard A. MabA (FabG1), a Mycobacterium tuberculosis protein involved in the long-chain fatty acid elongation system, FAS-II. Microbiology 148 (2002) 951-960
5. Vilchèze C., Morbidoni H.R., Weisbrod T.R., Iwamoto H., Kuo M., Sacchettini J.C., and Jacobs Jr. W.R. Inactivation of the inhA-encoded fatty acid synthase II (FASII) enoyl-acyl carrier protein reductase induces accumulation of the FASI end products and cell lysis of Mycobacterium smegmatis. J. Bacteriol. 182 (2000) 4059-4067
6. Rock C.O., and Cronan J.E. Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis. Biochim. Biophys. Acta 1302 (1996) 1-16
7. Bloch K. Control mechanisms for fatty acid synthesis in Mycobacterium smegmatis. Adv. Enzymol. 45 (1977) 1-84
8. Kikuchi S., and Kusaka T. New malonyl-CoA-dependent fatty acid elongation system in Mycobacterium smegmatis. J. Biochem. 92 (1982) 839-844
9. Kikuchi S., Takeuchi T., Yasui M., Kusaka T., and Kolattukudy P.E. A very long-chain fatty acid elongation system in Mycobacterium avium and a possible mode of action of isoniazid on the system. Agric. Biol. Chem. 53 (1989) 1689-1698
10. Quémard A., Sacchettini J.C., Dessen A., Vilchèze C., Bittman R., Jacobs Jr. W.R., and Blanchard J.S. Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis. Biochemistry 34 (1995) 8235-8241
11. Schaeffer M.L., Agnihotri G., Volker C., Kallender H., Brennan P.J., and Lonsdale J.T. Purification and biochemical characterisation of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthases, KasA and KasB. J. Biol. Chem. 276 (2001) 47029-47037
12. Kremer L., Dover L.G., Carrère S., Nampoothiri K.M., Lesjean S., Brown A.K., Brennan P.J., Minnikin D.E., Locht C., and Besra G.S. Mycolic acid biosynthesis and enzymatic characterization of the β-ketoacyl-ACP synthase A-condensing enzyme from Mycobacterium tuberculosis. Biochem. J. 364 (2002) 423-430
13. Joshi A.K., and Smith S. Construction, expression and characterization of a mutated animal fatty acid synthase deficient in the dehydrase function. J. Biol. Chem. 268 (1993) 22508-22513
14. Kostrewa D., Winkler F.K., Folkers G., Scapozza L., and Perozzo R. The crystal structure of PfFabZ, the unique beta-hydroxyacyl-ACP dehydratase involved in fatty acid biosynthesis of Plasmodium falciparum. Protein Sci. 14 (2005) 1570-1580
15. Wang H., and Cronan J.E. Functional replacement of the FabA and FabB proteins of Escherichia coli fatty acid synthesis by Enterococcus faecalis FabZ and FabF homologues. J. Biol. Chem. 279 (2004) 34489-34495
16. Jonassen I., Collins J.F., and Higgins D.G. Finding flexible patterns in unaligned protein sequences. Protein Sci. 4 (1995) 1587-1595
17. Gattiker A., Gasteiger E., and Bairoch A. ScanProsite: a reference implementation of a PROSITE scanning tool. Appl. Bioinformatics 1 (2002) 107-108
18. Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., Gordon S.V., Eiglmeier K., Gas S., Barry III C.E., Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L., Oliver K., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton J., Squares R., Squares S., Sulston J.E., Taylor K., Whitehead S., and Barrell B.G. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393 (1998) 537-544
19. Altschul S.F., Madden T.L., Schäffer A.A., Zhang J., Zhang Z., Miller W., and Lipman D.J. "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs". Nucleic Acids Res. 25 (1997) 3389-3402
20. Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
21. Corpet F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16 (1988) 10881-10890
22. Mulder N.J., Apweiler R., Attwood T.K., Bairoch A., Bateman A., Binns D., Bradley P., Bork P., Bucher P., Cerutti L., Copley R., Courcelle E., Das U., Durbin R., Fleischmann W., Gough J., Haft D., Harte N., Hulo N., Kahn D., Kanapin A., Krestyaninova M., Lonsdale D., Lopez R., Letunic I., Madera M., Maslen J., McDowall J., Mitchell A., Nikolskaya A.N., Orchard S., Pagni M., Ponting C.P., Quevillon E., Selengut J., Sigrist C.J., Silventoinen V., Studholme D.J., Vaughan R., and Wu C.H. InterPro, progress and status in 2005. Nucleic Acids Res. 33 (2005) D201-D205
23. Douguet D., and Labesse G. Easier threading through web-based comparisons and cross-validations. Bioinformatics 17 (2001) 752-753
24. Catherinot V., and Labesse G. ViTO: tool for refinement of protein sequence-structure alignments. Bioinformatics 20 (2004) 3694-3696
25. Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
26. Eisenberg D., Luthy R., and Bowie J.U. VERIFY3D: assessment of protein models with three-dimensional profiles. Methods Enzymol. 277 (1997) 396-404
27. Sippl M.J. Recognition of errors in three-dimensional structures of proteins. Proteins 17 (1993) 355-362
28. Schmid D., Jaussi R., and Christen P. Precursor of mitochondrial aspartate aminotransferase synthetized in Escherichia coli is complexed with heat-shock protein DnaK. Eur. J. Biochem. 208 (1992) 699-704
29. Besra G.S., Minnikin D.E., Wheeler P.R., and Ratledge C. Synthesis of methyl (Z)-tetracos-5-enoate and both enantiomers of ethyl (E)-6-methyltetracos-4-enoate: possible intermediates in the biosynthesis of mycolic acids in mycobacteria. Chem. Phys. Lipids 66 (1993) 23-34
30. Vagelos P.R., and Alberts A.W. Chemical synthesis of β-ketooctanoyl-coenzyme A. Anal. Biochem. 1 (1960) 8-16
31. Cronan Jr. J.E., and Klages A.L. Chemical synthesis of acyl thioesters of acyl carrier protein with native structure. Proc. Natl. Acad. Sci. 78 (1981) 5440-5444
32. Pelicic V., Jackson M., Reyrat J.-M., Jacobs Jr. W.R., Gicquel B., and Guilhot C. Efficient allelic exchange and transposon mutagenesis in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. 94 (1997) 10955-10960
33. Dubnau E., Chan J., Raynaud C., Mohan V.P., Lanéelle M.A., Yu K., Quémard A., Smith I., and Daffé M. Oxygenated mycolic acids are necessary for virulence of Mycobacterium tuberculosis in mice. Mol. Microbiol. 36 (2000) 630-637
34. Laval F., Lanéelle M.A., Déon C., Monsarrat B., and Daffé M. Accurate molecular mass determination of mycolic acids by MALDI-TOF mass spectrometry. Anal. Chem. 73 (2001) 4537-4544
35. Engel C.K., Mathieu M., Zeelen J.P., Hiltunen J.K., and 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. 15 (1996) 5135-5145
36. Leesong M., Henderson B.S., Gillig J.R., Schwab J.M., and Smith J.L. Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Structure 4 (1996) 253-264
37. Kimber M.S., Martin F., Lu Y., Houston S., Vedadi M., Dharamsi A., Fiebig K.M., Schmid M., and Rock C.O. The structure of (3R)-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Pseudomonas aeruginosa. J. Biol. Chem. 279 (2004) 52593-52602
38. Yuan Y., Lee R.E., Besra G.S., Belisle J.T., and Barry III C.E. Identification of a gene involved in the biosynthesis of cyclopropanated mycolic acids in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. 92 (1995) 6630-6634
39. Koski M.K., Haapalainen A.M., Hiltunen J.K., and Glumoff T. A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2. J. Biol. Chem. 279 (2004) 24666-24672
40. Hisano T., Tsuge T., Fukui T., Iwata T., Miki K., and Doi Y. Crystal structure of the (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis. J. Biol. Chem. 278 (2003) 617-624
41. Li J., Derewenda U., Dauter Z., Smith S., and Derewenda Z.S. Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme. Nat. Struct. Biol. 7 (2000) 555-559
42. Kass L.R., Brock D.J., and Bloch K. β-hydroxydecanoyl thioester dehydrase: I. Purification and properties. J. Biol. Chem. 242 (1967) 4418-4431
43. Castell A., Johansson P., Unge T., Jones T.A., and Bäckbro K. Rv0216, a conserved hypothetical protein from Mycobacterium tuberculosis that is essential for bacterial survival during infection, has a double hotdog fold. Protein Sci. 14 (2005) 1850-1862
44. Kastaniotis A.J., Autio K.J., Sormunen R.T., and Hiltunen J.K. Htd2p/Yhr067p is a yeast 3-hydroxyacyl-ACP dehydratase essential for mitochondrial function and morphology. Mol. Microbiol. 53 (2004) 1407-1421
45. Labesse G., Colloc'h N., Pothier J., and Mornon J.P. P-SEA: a new efficient assignment of secondary structure from C alpha trace of proteins. Comput. Appl. Biosci. 13 (1997) 291-295