메뉴 건너뛰기




Volumn 1794, Issue 7, 2009, Pages 1073-1081

Structure and function of a Campylobacter jejuni thioesterase Cj0915, a hexameric hot dog fold enzyme

Author keywords

Campylobacter jejuni; Crystal structure; Hot dog fold; Membrane lipid biosynthesis; Thioesterase

Indexed keywords

ACYL COENZYME A; BACTERIAL PROTEIN; CAMPYLOBACTER JEJUNI THIOL ESTER HYDROLASE; UNCLASSIFIED DRUG;

EID: 67349094267     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.03.002     Document Type: Article
Times cited : (15)

References (31)
  • 1
    • 0036138306 scopus 로고    scopus 로고
    • The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism
    • Hunt M.C., and Alexson S.E. The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism. Prog. Lipid Res. 41 (2002) 99-130
    • (2002) Prog. Lipid Res. , vol.41 , pp. 99-130
    • Hunt, M.C.1    Alexson, S.E.2
  • 2
    • 0032784276 scopus 로고    scopus 로고
    • Alpha/beta hydrolase fold enzymes: the family keeps growing
    • Nardini M., and Dijkstra B.W. Alpha/beta hydrolase fold enzymes: the family keeps growing. Curr. Opin. Struct. Biol. 9 (1999) 732-737
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 732-737
    • Nardini, M.1    Dijkstra, B.W.2
  • 3
    • 38149122142 scopus 로고    scopus 로고
    • Catalytic promiscuity in the alpha/beta-hydrolase superfamily: hydroxamic acid formation, C-C bond formation, ester and thioester hydrolysis in the C-C hydrolase family
    • Li C., Hassler M., and Bugg T.D. Catalytic promiscuity in the alpha/beta-hydrolase superfamily: hydroxamic acid formation, C-C bond formation, ester and thioester hydrolysis in the C-C hydrolase family. Chembiochem 9 (2008) 71-76
    • (2008) Chembiochem , vol.9 , pp. 71-76
    • Li, C.1    Hassler, M.2    Bugg, T.D.3
  • 4
    • 13244267005 scopus 로고    scopus 로고
    • The hotdog fold: wrapping up a superfamily of thioesterases and dehydratases
    • Dillon S.C., and Bateman A. The hotdog fold: wrapping up a superfamily of thioesterases and dehydratases. BMC Bioinformatics 5 (2004) 109
    • (2004) BMC Bioinformatics , vol.5 , pp. 109
    • Dillon, S.C.1    Bateman, A.2
  • 5
    • 0030584655 scopus 로고    scopus 로고
    • Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site
    • 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
    • (1996) Structure , vol.4 , pp. 253-264
    • Leesong, M.1    Henderson, B.S.2    Gillig, J.R.3    Schwab, J.M.4    Smith, J.L.5
  • 7
    • 35648945254 scopus 로고    scopus 로고
    • Campylobacter flagella: not just for motility
    • Guerry P. Campylobacter flagella: not just for motility. Trends Microbiol. 15 (2007) 456-461
    • (2007) Trends Microbiol. , vol.15 , pp. 456-461
    • Guerry, P.1
  • 8
    • 54849408203 scopus 로고    scopus 로고
    • Structure of a σ28-regulated nonflagellar virulence protein from Campylobacter jejuni
    • Yokoyama T., Paek S., Ewing C.P., Guerry P., and Yeo H.J. Structure of a σ28-regulated nonflagellar virulence protein from Campylobacter jejuni. J. Mol. Biol. 384 (2008) 364-376
    • (2008) J. Mol. Biol. , vol.384 , pp. 364-376
    • Yokoyama, T.1    Paek, S.2    Ewing, C.P.3    Guerry, P.4    Yeo, H.J.5
  • 11
    • 0033936807 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme
    • 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
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 555-559
    • Li, J.1    Derewenda, U.2    Dauter, Z.3    Smith, S.4    Derewenda, Z.S.5
  • 12
    • 0035155704 scopus 로고    scopus 로고
    • Organisation and evolution of the tol-pal gene cluster
    • Sturgis J.N. Organisation and evolution of the tol-pal gene cluster. J. Mol. Microbiol. Biotechnol. 3 (2001) 113-122
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 113-122
    • Sturgis, J.N.1
  • 13
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 14
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • Vagin A., and Teplyakov A. An approach to multi-copy search in molecular replacement. Acta Crystallogr. D 56 (2000) 1622-1624
    • (2000) Acta Crystallogr. D , vol.56 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2
  • 15
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 18
    • 0023790275 scopus 로고
    • A novel type of short- and medium-chain acyl-CoA hydrolases in brown adipose tissue mitochondria
    • Alexson S.E., and Nedergaard J. A novel type of short- and medium-chain acyl-CoA hydrolases in brown adipose tissue mitochondria. J. Biol. Chem. 263 (1988) 13564-13571
    • (1988) J. Biol. Chem. , vol.263 , pp. 13564-13571
    • Alexson, S.E.1    Nedergaard, J.2
  • 19
    • 40149083760 scopus 로고    scopus 로고
    • Structure of YciA from Haemophilus influenzae (HI0827), a hexameric broad specificity acyl-coenzyme A thioesterase
    • Willis M.A., Zhuang Z., Song F., Howard A., Dunaway-Mariano D., and Herzberg O. Structure of YciA from Haemophilus influenzae (HI0827), a hexameric broad specificity acyl-coenzyme A thioesterase. Biochemistry 47 (2008) 2797-2805
    • (2008) Biochemistry , vol.47 , pp. 2797-2805
    • Willis, M.A.1    Zhuang, Z.2    Song, F.3    Howard, A.4    Dunaway-Mariano, D.5    Herzberg, O.6
  • 20
    • 0032509337 scopus 로고    scopus 로고
    • The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. strain CBS-3
    • Benning M.M., Wesenberg G., Liu R., Taylor K.L., Dunaway-Mariano D., and Holden H.M. The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. strain CBS-3. J. Biol. Chem. 273 (1998) 33572-33579
    • (1998) J. Biol. Chem. , vol.273 , pp. 33572-33579
    • Benning, M.M.1    Wesenberg, G.2    Liu, R.3    Taylor, K.L.4    Dunaway-Mariano, D.5    Holden, H.M.6
  • 23
    • 0037178828 scopus 로고    scopus 로고
    • X-ray crystallographic analyses of inhibitor and substrate complexes of wild-type and mutant 4-hydroxybenzoyl-CoA thioesterase
    • Thoden J.B., Holden H.M., Zhuang Z., and Dunaway-Mariano D. X-ray crystallographic analyses of inhibitor and substrate complexes of wild-type and mutant 4-hydroxybenzoyl-CoA thioesterase. J. Biol. Chem. 277 (2002) 27468-27476
    • (2002) J. Biol. Chem. , vol.277 , pp. 27468-27476
    • Thoden, J.B.1    Holden, H.M.2    Zhuang, Z.3    Dunaway-Mariano, D.4
  • 24
    • 0242290213 scopus 로고    scopus 로고
    • The structure of 4-hydroxybenzoyl-CoA thioesterase from Arthrobacter sp. strain SU
    • Thoden J.B., Zhuang Z., Dunaway-Mariano D., and Holden H.M. The structure of 4-hydroxybenzoyl-CoA thioesterase from Arthrobacter sp. strain SU. J. Biol. Chem. 278 (2003) 43709-43716
    • (2003) J. Biol. Chem. , vol.278 , pp. 43709-43716
    • Thoden, J.B.1    Zhuang, Z.2    Dunaway-Mariano, D.3    Holden, H.M.4
  • 26
    • 0028871926 scopus 로고
    • Dali: a network tool for protein structure comparison
    • Holm L., and Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20 (1995) 478-480
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 27
    • 1542350187 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of ACH2, an acyl-CoA thioesterase from Arabidopsis thaliana
    • Tilton G.B., Shockey J.M., and Browse J. Biochemical and molecular characterization of ACH2, an acyl-CoA thioesterase from Arabidopsis thaliana. J. Biol. Chem. 279 (2004) 7487-7494
    • (2004) J. Biol. Chem. , vol.279 , pp. 7487-7494
    • Tilton, G.B.1    Shockey, J.M.2    Browse, J.3
  • 28
    • 2442705402 scopus 로고    scopus 로고
    • Secretion of virulence proteins from Campylobacter jejuni is dependent on a functional flagellar export apparatus
    • Konkel M.E., Klena J.D., Rivera-Amill V., Monteville M.R., Biswas D., Raphael B., and Mickelson J. Secretion of virulence proteins from Campylobacter jejuni is dependent on a functional flagellar export apparatus. J. Bacteriol. 186 (2004) 3296-3303
    • (2004) J. Bacteriol. , vol.186 , pp. 3296-3303
    • Konkel, M.E.1    Klena, J.D.2    Rivera-Amill, V.3    Monteville, M.R.4    Biswas, D.5    Raphael, B.6    Mickelson, J.7
  • 29
    • 0037051944 scopus 로고    scopus 로고
    • The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster of Haemophilus influenzae catalyzes acyl-coenzyme A thioester hydrolysis
    • Zhuang Z., Song F., Martin B.M., and Dunaway-Mariano D. The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster of Haemophilus influenzae catalyzes acyl-coenzyme A thioester hydrolysis. FEBS Lett. 516 (2002) 161-163
    • (2002) FEBS Lett. , vol.516 , pp. 161-163
    • Zhuang, Z.1    Song, F.2    Martin, B.M.3    Dunaway-Mariano, D.4
  • 30
    • 4344684651 scopus 로고    scopus 로고
    • X-ray structure analysis of a designed oligomeric miniprotein reveals a discrete quaternary architecture
    • Ali M.H., Peisach E., Allen K.N., and Imperiali B. X-ray structure analysis of a designed oligomeric miniprotein reveals a discrete quaternary architecture. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 12183-12188
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 12183-12188
    • Ali, M.H.1    Peisach, E.2    Allen, K.N.3    Imperiali, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.