메뉴 건너뛰기




Volumn 349, Issue 1, 2006, Pages 172-177

Crystal structure of human thioesterase superfamily member 2

Author keywords

Active site; Crystal structure; Hotdog fold; hTHEM2; PaaI; Substrate screening; Thioesterase

Indexed keywords

ASPARTIC ACID; BACTERIAL PROTEIN; HUMAN THIOESTERASE SUPERFAMILY MEMBER 2; HYDROLASE; PAAI PROTEIN; PHENYLACETYL COENZYME A HYDROLASE; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; TETRAMER; THIOL ESTER HYDROLASE; UNCLASSIFIED DRUG;

EID: 33748323250     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.08.025     Document Type: Article
Times cited : (30)

References (25)
  • 2
    • 0037883296 scopus 로고    scopus 로고
    • Characterization of the 4-hydroxybenzoyl-coenzyme A thioesterase from Arthrobacter sp. strain SU
    • Zhuang Z., Gartemann K.H., Eichenlaub R., and Dunaway-Mariano D. Characterization of the 4-hydroxybenzoyl-coenzyme A thioesterase from Arthrobacter sp. strain SU. Appl. Environ. Microbiol. 69 (2003) 2707-2711
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 2707-2711
    • Zhuang, Z.1    Gartemann, K.H.2    Eichenlaub, R.3    Dunaway-Mariano, D.4
  • 3
    • 0032476062 scopus 로고    scopus 로고
    • Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway
    • Ferrandez A., Minambres B., Garcia B., Olivera E.R., Luengo J.M., Garcia J.L., and Diaz E. Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. J. Biol. Chem. 273 (1998) 25974-25986
    • (1998) J. Biol. Chem. , vol.273 , pp. 25974-25986
    • Ferrandez, A.1    Minambres, B.2    Garcia, B.3    Olivera, E.R.4    Luengo, J.M.5    Garcia, J.L.6    Diaz, E.7
  • 4
    • 12144262058 scopus 로고    scopus 로고
    • Aberrant cytosolic acyl-CoA thioester hydrolase in hippocampus of patients with mesial temporal lobe epilepsy
    • Yang J.W., Czech T., Yamada J., Csaszar E., Baumgartner C., Slavc I., and Lubec G. Aberrant cytosolic acyl-CoA thioester hydrolase in hippocampus of patients with mesial temporal lobe epilepsy. Amino Acids 27 (2004) 269-275
    • (2004) Amino Acids , vol.27 , pp. 269-275
    • Yang, J.W.1    Czech, T.2    Yamada, J.3    Csaszar, E.4    Baumgartner, C.5    Slavc, I.6    Lubec, G.7
  • 7
    • 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
  • 10
    • 0036900870 scopus 로고    scopus 로고
    • Rapid automatic NCS identification using heavy-atom substructures
    • Terwilliger T.C. Rapid automatic NCS identification using heavy-atom substructures. Acta Crystallogr. D Biol. Crystallogr. 58 (2002) 2213-2215
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , pp. 2213-2215
    • Terwilliger, T.C.1
  • 13
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski M.W.M.R.A., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26 (1993) 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, M.W.M.R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 15
    • 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
  • 16
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., and Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233 (1993) 123-138
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 17
    • 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
  • 18
    • 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
  • 19
    • 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
  • 21
    • 0035951110 scopus 로고    scopus 로고
    • Role of active site binding interactions in 4-chlorobenzoyl-coenzyme A dehalogenase catalysis
    • Luo L., Taylor K.L., Xiang H., Wei Y., Zhang W., and Dunaway-Mariano D. Role of active site binding interactions in 4-chlorobenzoyl-coenzyme A dehalogenase catalysis. Biochemistry 40 (2001) 15684-15692
    • (2001) Biochemistry , vol.40 , pp. 15684-15692
    • Luo, L.1    Taylor, K.L.2    Xiang, H.3    Wei, Y.4    Zhang, W.5    Dunaway-Mariano, D.6
  • 24
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 25
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., and Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.