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Volumn 325, Issue 1, 2004, Pages 10-17

Erratum: (Retracted article): Interaction of shikimic acid with shikimate kinase (Biochemical and Biophysical Research Communications (2004) 325 (10-17) DOI: 10.1016/j.bbrc.2004.09.217);Interaction of shikimic acid with shikimate kinase

Author keywords

Drug design; Mycobacterium tuberculosis; Shikimate kinase; Shikimic acid; Structure

Indexed keywords

ADENOSINE DIPHOSPHATE; AMINO ACID; ARGININE; ASPARTIC ACID; CARBOXYL GROUP; GLUTAMINE; GLYCINE; GUANIDINE; HYDROXYL GROUP; ISOENZYME; MAGNESIUM DERIVATIVE; SHIKIMATE KINASE; SHIKIMIC ACID; UNCLASSIFIED DRUG;

EID: 7444250740     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.06.159     Document Type: Erratum
Times cited : (5)

References (36)
  • 1
    • 0028967182 scopus 로고
    • A reassessment of the relationship between aroK- and aroL-encoded shikimate kinase enzymes of Escherichia coli
    • M.J. Whipp, and A.J. Pittard A reassessment of the relationship between aroK- and aroL-encoded shikimate kinase enzymes of Escherichia coli J. Bacteriol. 177 1995 1627 1629
    • (1995) J. Bacteriol. , vol.177 , pp. 1627-1629
    • Whipp, M.J.1    Pittard, A.J.2
  • 2
    • 0022474607 scopus 로고
    • The cloning and expression of the aroL gene from Escherichia coli K-12
    • G. Millar, A. Lewendon, M.G. Hunter, and J.R Coggins The cloning and expression of the aroL gene from Escherichia coli K-12 Biochem. J. 237 1986 427 437
    • (1986) Biochem. J. , vol.237 , pp. 427-437
    • Millar, G.1    Lewendon, A.2    Hunter, M.G.3    Coggins, J.R.4
  • 3
    • 0022483540 scopus 로고
    • Purification and properties of shikimate kinase II from Escherichia coli K-12
    • R.C. De Feyter, and J. Pittard Purification and properties of shikimate kinase II from Escherichia coli K-12 J. Bacteriol. 165 1986 331 333
    • (1986) J. Bacteriol. , vol.165 , pp. 331-333
    • De Feyter, R.C.1    Pittard, J.2
  • 4
    • 0018392983 scopus 로고
    • Aromatic amino acid biosynthesis: Regulation of shikimate kinase in Escherichia coli K-12
    • B. Ely, and J. Pittard Aromatic amino acid biosynthesis: regulation of shikimate kinase in Escherichia coli K-12 J. Bacteriol. 138 1979 933 943
    • (1979) J. Bacteriol. , vol.138 , pp. 933-943
    • Ely, B.1    Pittard, J.2
  • 5
    • 0022548992 scopus 로고
    • Nucleotide sequences of the transcription unit containing the aroL and aroM genes from Escherichia coli K-12
    • R.C. De Feyter, B.E. Davidson, and J. Pittard Nucleotide sequences of the transcription unit containing the aroL and aroM genes from Escherichia coli K-12 J. Bacteriol. 165 1986 233 239
    • (1986) J. Bacteriol. , vol.165 , pp. 233-239
    • De Feyter, R.C.1    Davidson, B.E.2    Pittard, J.3
  • 6
    • 0029991644 scopus 로고    scopus 로고
    • Mecillinam resistance in Escherichia coli is conferred by loss of a second activity of the aroK protein
    • D. Vinella, B. Gagny, D. Joseleau-Petit, R. D'Ardi, and M. Cashel Mecillinam resistance in Escherichia coli is conferred by loss of a second activity of the aroK protein J. Bacteriol. 178 1996 3818 3828
    • (1996) J. Bacteriol. , vol.178 , pp. 3818-3828
    • Vinella, D.1    Gagny, B.2    Joseleau-Petit, D.3    D'Ardi, R.4    Cashel, M.5
  • 7
    • 0036300993 scopus 로고    scopus 로고
    • Crystal structure of shikimate kinase from Mycobacterium tuberculosis reveals the dynamic role of the LID domain in catalysis
    • Y. Gu, L. Reshetnikova, Y. Li, Y. Wu, H. Yan, S. Singh, and X. Ji Crystal structure of shikimate kinase from Mycobacterium tuberculosis reveals the dynamic role of the LID domain in catalysis J. Mol. Biol. 319 2002 779 789
    • (2002) J. Mol. Biol. , vol.319 , pp. 779-789
    • Gu, Y.1    Reshetnikova, L.2    Li, Y.3    Wu, Y.4    Yan, H.5    Singh, S.6    Ji, X.7
  • 8
    • 0032557708 scopus 로고    scopus 로고
    • The three-dimensional structure of shikimate kinase
    • T. Krell, J.R. Coggins, and A.J. Lapthorn The three-dimensional structure of shikimate kinase J. Mol. Biol. 278 1998 983 997
    • (1998) J. Mol. Biol. , vol.278 , pp. 983-997
    • Krell, T.1    Coggins, J.R.2    Lapthorn, A.J.3
  • 9
    • 0035008584 scopus 로고    scopus 로고
    • Biochemical and X-ray crystallographic studies on shikimate kinase: The important structural role of the P-loop lysine
    • T. Krell, J. Maclean, D.J. Boam, A. Cooper, M. Resmini, and K. Brocklehurst Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine Protein Sci. 10 2001 1137 1149
    • (2001) Protein Sci. , vol.10 , pp. 1137-1149
    • Krell, T.1    MacLean, J.2    Boam, D.J.3    Cooper, A.4    Resmini, M.5    Brocklehurst, K.6
  • 10
    • 0023887425 scopus 로고
    • Refined structure of porcine cytosolic adenylate kinase at 2.1 Å resolution
    • D. Dreusicke, A. Karplus, and G.E. Schulz Refined structure of porcine cytosolic adenylate kinase at 2.1 Å resolution J. Mol. Biol. 199 1988 359 371
    • (1988) J. Mol. Biol. , vol.199 , pp. 359-371
    • Dreusicke, D.1    Karplus, A.2    Schulz, G.E.3
  • 11
    • 0029897810 scopus 로고    scopus 로고
    • The structure of bovine mitochondrial adenylate kinase: Comparison with isoenzymes in other compartments
    • G.J. Schlauderer, and G.E. Schulz The structure of bovine mitochondrial adenylate kinase: comparison with isoenzymes in other compartments Protein Sci. 5 1996 434 441
    • (1996) Protein Sci. , vol.5 , pp. 434-441
    • Schlauderer, G.J.1    Schulz, G.E.2
  • 12
    • 0025012803 scopus 로고
    • Three-dimensional structure of the complex of guanylate kinase from yeast with its substrate GMP
    • T. Stehle, and G.E. Schulz Three-dimensional structure of the complex of guanylate kinase from yeast with its substrate GMP J. Mol. Biol. 211 1990 249 254
    • (1990) J. Mol. Biol. , vol.211 , pp. 249-254
    • Stehle, T.1    Schulz, G.E.2
  • 13
    • 0028327709 scopus 로고
    • The structure of uridylate kinase with its substrates, showing the transition state geometry
    • H.-J. Müller-Dieckmann, and G.E. Schulz The structure of uridylate kinase with its substrates, showing the transition state geometry J. Mol. Biol. 236 1994 361 367
    • (1994) J. Mol. Biol. , vol.236 , pp. 361-367
    • Müller-Dieckmann, H.-J.1    Schulz, G.E.2
  • 14
    • 0029020644 scopus 로고
    • The three-dimensional structure of thymidine kinase from Herpes simplex virus type 1
    • K. Wild, T. Bohner, A. Aubry, G. Folkers, and G.E. Schulz The three-dimensional structure of thymidine kinase from Herpes simplex virus type 1 FEBS Lett. 368 1995 289 292
    • (1995) FEBS Lett. , vol.368 , pp. 289-292
    • Wild, K.1    Bohner, T.2    Aubry, A.3    Folkers, G.4    Schulz, G.E.5
  • 15
    • 0029644728 scopus 로고
    • Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases
    • C. Vonrhein, G.J. Schlauderer, and G.E. Schulz Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases Structure 3 1995 483 490
    • (1995) Structure , vol.3 , pp. 483-490
    • Vonrhein, C.1    Schlauderer, G.J.2    Schulz, G.E.3
  • 16
    • 0029644168 scopus 로고    scopus 로고
    • Adenylate kinase motions during catalysis: An energetic counterweight balancing substrate binding
    • C.W. Müller, G.J. Schlauderer, J. Reinstein, and G.E. Schulz Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding Structure 4 1996 147 156
    • (1996) Structure , vol.4 , pp. 147-156
    • Müller, C.W.1    Schlauderer, G.J.2    Reinstein, J.3    Schulz, G.E.4
  • 17
    • 0027528934 scopus 로고
    • Domain closure in adenylate kinase: Joints on either side of two helices close like neighbouring fingers
    • M. Gerstein, G.E. Schulz, and C. Chothia Domain closure in adenylate kinase: joints on either side of two helices close like neighbouring fingers J. Mol. Biol. 229 1993 494 501
    • (1993) J. Mol. Biol. , vol.229 , pp. 494-501
    • Gerstein, M.1    Schulz, G.E.2    Chothia, C.3
  • 18
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • J.E. Walker, M. Saraste, M.J. Runswick, and N.J. Gay Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold EMBO J. 1 1982 945 951
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 19
    • 0029914905 scopus 로고    scopus 로고
    • Active site comparisons highlight structural similarities between myosin and other P-loop proteins
    • C.A. Smith, and I. Rayment Active site comparisons highlight structural similarities between myosin and other P-loop proteins Biophys. J. 70 1996 1590 1602
    • (1996) Biophys. J. , vol.70 , pp. 1590-1602
    • Smith, C.A.1    Rayment, I.2
  • 20
    • 0142011067 scopus 로고    scopus 로고
    • Evolution and classification of P-loop kinases and related proteins
    • D.D. Leipe, E.V. Koonin, and L. Aravind Evolution and classification of P-loop kinases and related proteins J. Mol. Biol. 333 2003 781 815
    • (2003) J. Mol. Biol. , vol.333 , pp. 781-815
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 23
    • 0028103275 scopus 로고
    • Collaborative Computational Project 4 the CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project 4 The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D50 (1994) 760-763
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 24
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallogr. A 50 1994 157 163
    • (1994) Acta Crystallogr. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 26
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density
    • D.E. McRee XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density J. Struct. Biol. 125 1999 156 165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 28
    • 0030587517 scopus 로고    scopus 로고
    • The crystal structure of the bifunctional enzyme 6-phosphofructo-2- kinase/fructose-2,6-biphosphatase reveals distinct domain homologies
    • C.A. Hasemann, E.S. Istvan, K. Uyeda, and J. Deisenhofer The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6- biphosphatase reveals distinct domain homologies Structure 4 1996 1017 1029
    • (1996) Structure , vol.4 , pp. 1017-1029
    • Hasemann, C.A.1    Istvan, E.S.2    Uyeda, K.3    Deisenhofer, J.4
  • 29
    • 0036606577 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to Mecillinam
    • M.J. Romanowski, and S.K. Burley Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to Mecillinam Proteins: Struct Funct. Genet. 47 2002 558 562
    • (2002) Proteins: Struct Funct. Genet. , vol.47 , pp. 558-562
    • Romanowski, M.J.1    Burley, S.K.2
  • 30
    • 0016624901 scopus 로고
    • Binding energy, specificity and enzymatic catalysis: The circe effect
    • W.P. Jencks Binding energy, specificity and enzymatic catalysis: the circe effect Adv. Enzymol. 43 1975 219 410
    • (1975) Adv. Enzymol. , vol.43 , pp. 219-410
    • Jencks, W.P.1
  • 31
    • 0035207956 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of shikimate kinase from Mycobacterium tuberculosis in complex with MgADP
    • Y. Gu, L. Reshetnikova, Y. Li, H. Yan, S.V. Singh, and X. Ji Crystallization and preliminary X-ray diffraction analysis of shikimate kinase from Mycobacterium tuberculosis in complex with MgADP Acta Crystallogr. D57 2001 1870 1871
    • (2001) Acta Crystallogr. , vol.57 , pp. 1870-1871
    • Gu, Y.1    Reshetnikova, L.2    Li, Y.3    Yan, H.4    Singh, S.V.5    Ji, X.6
  • 35
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wüthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 36
    • 4444331458 scopus 로고    scopus 로고
    • Crystallographic studies of shikimate binding and induced conformational changes in Mycobacterium tuberculosis shikimate kinase
    • B. Dhaliwal, C.E. Nichols, J. Ren, M. Lockyer, I. Charles, A.R. Hawkins, D.K. Stammers, Crystallographic studies of shikimate binding and induced conformational changes in Mycobacterium tuberculosis shikimate kinase, FEBS Lett. (2004)
    • (2004) FEBS Lett.
    • Dhaliwal, B.1    Nichols, C.E.2    Ren, J.3    Lockyer, M.4    Charles, I.5    Hawkins, A.R.6    Stammers, D.K.7


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