메뉴 건너뛰기




Volumn 343, Issue 3, 2004, Pages 671-684

Structures of unliganded and inhibitor complexes of W168F, a loop6 hinge mutant of Plasmodium falciparum triosephosphate isomerase: Observation of an intermediate position of loop6

Author keywords

catalytic loop6; flexibility; Plasmodium falciparum; triosephosphate isomerase; tryptophan mutant

Indexed keywords

GLYCEROL 2 PHOSPHATE; LIGAND; SULFATE; TRIOSEPHOSPHATE ISOMERASE;

EID: 4744356790     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.08.060     Document Type: Article
Times cited : (15)

References (40)
  • 1
    • 0035815109 scopus 로고    scopus 로고
    • The importance of hinge sequence for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase
    • J. Xiang, J. Sun, and N.S. Sampson The importance of hinge sequence for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase J. Mol. Biol. 307 2001 1103 1112
    • (2001) J. Mol. Biol. , vol.307 , pp. 1103-1112
    • Xiang, J.1    Sun, J.2    Sampson, N.S.3
  • 2
    • 0345894320 scopus 로고    scopus 로고
    • Active site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation
    • R. Desamero, S. Rozovsky, N. Zhadin, A. McDermott, and R. Callender Active site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation Biochemistry 42 2003 2941 2951
    • (2003) Biochemistry , vol.42 , pp. 2941-2951
    • Desamero, R.1    Rozovsky, S.2    Zhadin, N.3    McDermott, A.4    Callender, R.5
  • 3
    • 0033621030 scopus 로고    scopus 로고
    • Understanding protein lids: Kinetic analysis of active hinge mutants in triosephosphate isomerase
    • J. Sun, and N.S. Sampson Understanding protein lids: kinetic analysis of active hinge mutants in triosephosphate isomerase Biochemistry 38 1999 11474 11481
    • (1999) Biochemistry , vol.38 , pp. 11474-11481
    • Sun, J.1    Sampson, N.S.2
  • 4
    • 0025276041 scopus 로고
    • Stabilization of a reaction intermediate as a catalytic device: Definition of the functional role of the flexible loop in triosephosphate isomerase
    • D.L. Pompliano, A. Peyman, and J.R. Knowles Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase Biochemistry 29 1990 3186 3194
    • (1990) Biochemistry , vol.29 , pp. 3186-3194
    • Pompliano, D.L.1    Peyman, A.2    Knowles, J.R.3
  • 5
    • 0026779802 scopus 로고
    • Segmental movement: Definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase
    • N.S. Sampson, and J.R. Knowles Segmental movement: definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase Biochemistry 31 1992 8482 8487
    • (1992) Biochemistry , vol.31 , pp. 8482-8487
    • Sampson, N.S.1    Knowles, J.R.2
  • 6
    • 0037293775 scopus 로고    scopus 로고
    • Unusual fluorescence of W168 in Plasmodium falciparum triosephosphate isomerase, probed by single-tryptophan mutants
    • P. Pattanaik, G. Ravindra, C. Sengupta, K. Maithal, P. Balaram, and H. Balaram Unusual fluorescence of W168 in Plasmodium falciparum triosephosphate isomerase, probed by single-tryptophan mutants Eur. J. Biochem. 270 2003 745 756
    • (2003) Eur. J. Biochem. , vol.270 , pp. 745-756
    • Pattanaik, P.1    Ravindra, G.2    Sengupta, C.3    Maithal, K.4    Balaram, P.5    Balaram, H.6
  • 7
    • 0029000872 scopus 로고
    • Dynamics of the flexible loop of triosephosphate isomerase: The loop motion is not ligand gated
    • J.C. Williams, and A.E. McDermott Dynamics of the flexible loop of triosephosphate isomerase: the loop motion is not ligand gated Biochemistry 34 1995 8309 8319
    • (1995) Biochemistry , vol.34 , pp. 8309-8319
    • Williams, J.C.1    McDermott, A.E.2
  • 9
    • 0027081843 scopus 로고
    • Structure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phosphono-butanamide: Binding at the active site despite an "open" flexible loop conformation
    • C.L. Verlinde, C.J. Witmans, T. Pijning, K.H. Kalk, W.G. Hol, M. Callens, and F.R. Opperdoes Structure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phosphono-butanamide: binding at the active site despite an "open" flexible loop conformation Protein Sci. 1 1992 1578 1584
    • (1992) Protein Sci. , vol.1 , pp. 1578-1584
    • Verlinde, C.L.1    Witmans, C.J.2    Pijning, T.3    Kalk, K.H.4    Hol, W.G.5    Callens, M.6    Opperdoes, F.R.7
  • 10
    • 0035967856 scopus 로고    scopus 로고
    • Solution-state NMR investigations of triosephosphate isomerase active site loop motion: Ligand release in relation to active site loop dynamics
    • S. Rozovsky, G. Jogl, L. Tong, and A.E. McDermott Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics J. Mol. Biol. 310 2001 271 280
    • (2001) J. Mol. Biol. , vol.310 , pp. 271-280
    • Rozovsky, S.1    Jogl, G.2    Tong, L.3    McDermott, A.E.4
  • 11
    • 0031820040 scopus 로고    scopus 로고
    • Determination of the amino acid requirements for a protein hinge in triosephosphate isomerase
    • J. Sun, and N.S. Sampson Determination of the amino acid requirements for a protein hinge in triosephosphate isomerase Protein Sci. 7 1998 1495 1505
    • (1998) Protein Sci. , vol.7 , pp. 1495-1505
    • Sun, J.1    Sampson, N.S.2
  • 12
    • 0036899889 scopus 로고    scopus 로고
    • Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: Observation of the catalytic loop in the open conformation in the ligand-bound state
    • S. Parthasarathy, H. Balaram, P. Balaram, and M.R. Murthy Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: observation of the catalytic loop in the open conformation in the ligand-bound state Acta Crystallog. sect. D 58 2002 1992 2000
    • (2002) Acta Crystallog. Sect. D , vol.58 , pp. 1992-2000
    • Parthasarathy, S.1    Balaram, H.2    Balaram, P.3    Murthy, M.R.4
  • 13
    • 0037027339 scopus 로고    scopus 로고
    • Structure of the Plasmodium falciparum triosephosphate isomerase-phosphoglycolate complex in two crystal forms: Characterization of catalytic loop open and closed conformations in the ligand-bound state
    • S. Parthasarathy, G. Ravindra, H. Balaram, P. Balaram, and M.R. Murthy Structure of the Plasmodium falciparum triosephosphate isomerase- phosphoglycolate complex in two crystal forms: characterization of catalytic loop open and closed conformations in the ligand-bound state Biochemistry 41 2002 13178 13188
    • (2002) Biochemistry , vol.41 , pp. 13178-13188
    • Parthasarathy, S.1    Ravindra, G.2    Balaram, H.3    Balaram, P.4    Murthy, M.R.5
  • 14
    • 0346732297 scopus 로고    scopus 로고
    • Structure of Plasmodium falciparum TIM-2-phosphoglycerate complex at 1.1 Å resolution
    • S. Parthasarathy, K. Eaazhisai, H. Balaram, P. Balaram, and M.R. Murthy Structure of Plasmodium falciparum TIM-2-phosphoglycerate complex at 1.1 Å resolution J. Biol. Chem. 278 2003 52461 52470
    • (2003) J. Biol. Chem. , vol.278 , pp. 52461-52470
    • Parthasarathy, S.1    Eaazhisai, K.2    Balaram, H.3    Balaram, P.4    Murthy, M.R.5
  • 15
    • 0025882523 scopus 로고
    • The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes
    • M.E. Noble, R.K. Wierenga, A.M. Lambeir, F.R. Opperdoes, A.M. Thunnissen, and K.H. Kalk The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes Proteins: Struct. Funct. Genet. 10 1991 50 69
    • (1991) Proteins: Struct. Funct. Genet. , vol.10 , pp. 50-69
    • Noble, M.E.1    Wierenga, R.K.2    Lambeir, A.M.3    Opperdoes, F.R.4    Thunnissen, A.M.5    Kalk, K.H.6
  • 16
    • 0028846686 scopus 로고
    • Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions
    • L.F. Delboni, S.C. Mande, F. Rentier-Delrue, V. Mainfroid, S. Turley, and F.M. Vellieux Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions Protein Sci. 4 1995 2594 2604
    • (1995) Protein Sci. , vol.4 , pp. 2594-2604
    • Delboni, L.F.1    Mande, S.C.2    Rentier-Delrue, F.3    Mainfroid, V.4    Turley, S.5    Vellieux, F.M.6
  • 17
    • 0028298146 scopus 로고
    • Crystal structure of recombinant human triosephosphate isomerase at 2.8 Å resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme
    • S.C. Mande, V. Mainfroid, K.H. Kalk, K. Goraj, J.A. Martial, and W.G. Hol Crystal structure of recombinant human triosephosphate isomerase at 2.8 Å resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme Protein Sci. 3 1994 810 821
    • (1994) Protein Sci. , vol.3 , pp. 810-821
    • Mande, S.C.1    Mainfroid, V.2    Kalk, K.H.3    Goraj, K.4    Martial, J.A.5    Hol, W.G.6
  • 18
    • 0029645123 scopus 로고
    • Three new crystal structures of point mutation variants of monoTIM: Conformational flexibility of loop-1, loop-4 and loop-8
    • T.V. Borchert, K.V. Kishan, J.P. Zeelen, W. Schliebs, N. Thanki, and R. Abagyan Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8 Structure 3 1995 669 679
    • (1995) Structure , vol.3 , pp. 669-679
    • Borchert, T.V.1    Kishan, K.V.2    Zeelen, J.P.3    Schliebs, W.4    Thanki, N.5    Abagyan, R.6
  • 19
    • 0037984337 scopus 로고    scopus 로고
    • Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-Å resolution
    • I. Kursula, and R.K. Wierenga Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-Å resolution J. Biol. Chem. 278 2003 9544 9551
    • (2003) J. Biol. Chem. , vol.278 , pp. 9544-9551
    • Kursula, I.1    Wierenga, R.K.2
  • 20
    • 0025331920 scopus 로고
    • Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-Å resolution: Implications for catalysis
    • E. Lolis, and G.A. Petsko Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-Å resolution: implications for catalysis Biochemistry 29 1990 6619 6625
    • (1990) Biochemistry , vol.29 , pp. 6619-6625
    • Lolis, E.1    Petsko, G.A.2
  • 21
    • 0026056393 scopus 로고
    • Crystallographic and molecular modeling studies on trypanosomal triosephosphate isomerase: A critical assessment of the predicted and observed structures of the complex with 2-phosphoglycerate
    • M.E. Noble, C.L. Verlinde, H. Groendijk, K.H. Kalk, R.K. Wierenga, and W.G. Hol Crystallographic and molecular modeling studies on trypanosomal triosephosphate isomerase: a critical assessment of the predicted and observed structures of the complex with 2-phosphoglycerate J. Med. Chem. 34 1991 2709 2718
    • (1991) J. Med. Chem. , vol.34 , pp. 2709-2718
    • Noble, M.E.1    Verlinde, C.L.2    Groendijk, H.3    Kalk, K.H.4    Wierenga, R.K.5    Hol, W.G.6
  • 22
    • 0016797484 scopus 로고
    • The influence of pH on the interaction of inhibitors with triosephosphate isomerase and determination of the pKa of the active-site carboxyl group
    • F.C. Hartman, G.M. LaMuraglia, Y. Tomozawa, and R. Wolfenden The influence of pH on the interaction of inhibitors with triosephosphate isomerase and determination of the pKa of the active-site carboxyl group Biochemistry 14 1975 5274 5279
    • (1975) Biochemistry , vol.14 , pp. 5274-5279
    • Hartman, F.C.1    Lamuraglia, G.M.2    Tomozawa, Y.3    Wolfenden, R.4
  • 24
    • 0025331920 scopus 로고
    • Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5 Å resolution: Implications for catalysis
    • E. Lolis, and G.A. Petsko Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5 Å resolution: implications for catalysis Biochemistry 29 1990 6619 6625
    • (1990) Biochemistry , vol.29 , pp. 6619-6625
    • Lolis, E.1    Petsko, G.A.2
  • 25
    • 0025015392 scopus 로고
    • Anatomy of a conformational change: Hinged "lid" motion of the triosephosphate isomerase loop
    • D. Joseph, G.A. Petsko, and M. Karplus Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop Science 249 1990 1425 1428
    • (1990) Science , vol.249 , pp. 1425-1428
    • Joseph, D.1    Petsko, G.A.2    Karplus, M.3
  • 26
    • 0031972864 scopus 로고    scopus 로고
    • The loop opening/closing motion of the enzyme triosephosphate isomerase
    • P. Derreumaux, and T. Schlick The loop opening/closing motion of the enzyme triosephosphate isomerase Biophys. J. 74 1998 72 81
    • (1998) Biophys. J. , vol.74 , pp. 72-81
    • Derreumaux, P.1    Schlick, T.2
  • 27
    • 0344441463 scopus 로고    scopus 로고
    • Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: Evidence of conformational heterogeneity
    • R. Aparicio, S.T. Ferreira, and I. Polikarpov Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity J. Mol. Biol. 334 2003 1023 1041
    • (2003) J. Mol. Biol. , vol.334 , pp. 1023-1041
    • Aparicio, R.1    Ferreira, S.T.2    Polikarpov, I.3
  • 28
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowsky, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowsky, Z.1    Minor, W.2
  • 29
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallog. sect. A 50 1994 157 163
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 30
    • 0031053055 scopus 로고    scopus 로고
    • AMoRe: An automated molecular replacement program package
    • J. Navaza, and P. Saludjian AMoRe: an automated molecular replacement program package Methods Enzymol. 276 1997 581 593
    • (1997) Methods Enzymol. , vol.276 , pp. 581-593
    • Navaza, J.1    Saludjian, P.2
  • 31
    • 0031570683 scopus 로고    scopus 로고
    • Triosephosphate isomerase from Plasmodium falciparum: The crystal structure provides insights into antimalarial drug design
    • S.S. Velanker, S.S. Ray, R.S. Gokhale, S. Suma, H. Balaram, P. Balaram, and M.R. Murthy Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design Structure 5 1997 751 761
    • (1997) Structure , vol.5 , pp. 751-761
    • Velanker, S.S.1    Ray, S.S.2    Gokhale, R.S.3    Suma, S.4    Balaram, H.5    Balaram, P.6    Murthy, M.R.7
  • 32
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 35
    • 0028209049 scopus 로고
    • Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-Å resolution
    • Z. Zhang, S. Sugio, E.A. Komives, K.D. Liu, J.R. Knowles, G.A. Petsko, and D. Ringe Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-Å resolution Biochemistry 33 1994 2830 2837
    • (1994) Biochemistry , vol.33 , pp. 2830-2837
    • Zhang, Z.1    Sugio, S.2    Komives, E.A.3    Liu, K.D.4    Knowles, J.R.5    Petsko, G.A.6    Ringe, D.7
  • 36
    • 0025882959 scopus 로고
    • Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: An analogue of the intermediate on the reaction pathway
    • R.C. Davenport, P.A. Bash, B.A. Seaton, M. Karplus, G.A. Petsko, and D. Ringe Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway Biochemistry 30 1991 5821 5826
    • (1991) Biochemistry , vol.30 , pp. 5821-5826
    • Davenport, R.C.1    Bash, P.A.2    Seaton, B.A.3    Karplus, M.4    Petsko, G.A.5    Ringe, D.6
  • 37
    • 0037422593 scopus 로고    scopus 로고
    • Optimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2-Å resolution
    • G. Jogl, S. Rozovsky, A.E. McDermott, and L. Tong Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-Å resolution Proc. Natl Acad. Sci. USA 100 2003 50 55
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 50-55
    • Jogl, G.1    Rozovsky, S.2    McDermott, A.E.3    Tong, L.4
  • 38
    • 0001679473 scopus 로고    scopus 로고
    • ALIGN: A program to superimpose protein coordinates accounting for insertions and deletions
    • G.E. Cohen ALIGN: a program to superimpose protein coordinates accounting for insertions and deletions J. Appl. Crystallog. 30 1997 1160 1161
    • (1997) J. Appl. Crystallog. , vol.30 , pp. 1160-1161
    • Cohen, G.E.1
  • 39
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 40
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • E.A. Merritt, and D.J. Bacon Raster3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.