메뉴 건너뛰기




Volumn 8, Issue 1, 2000, Pages 35-46

The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: Implications for substrate channeling in a bifunctional enzyme

Author keywords

Bifunctional enzyme; Formiminotransferase cyclodeaminase; Substrate channeling; Tetrahydrofolate; X ray diffraction

Indexed keywords

ENZYME; FOLINIC ACID; FORMIMINOGLUTAMIC ACID; GLUTAMIC ACID; TETRAHYDROFOLIC ACID;

EID: 0034650448     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00078-2     Document Type: Article
Times cited : (41)

References (35)
  • 3
    • 0031028212 scopus 로고    scopus 로고
    • Protein architecture, dynamics and allostery in tryptophan synthase channeling
    • Pan P., Woehl E., Dunn M.F. Protein architecture, dynamics and allostery in tryptophan synthase channeling. Trends Biochem. Sci. 22:1997;22-27.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 22-27
    • Pan, P.1    Woehl, E.2    Dunn, M.F.3
  • 4
    • 0030957783 scopus 로고    scopus 로고
    • Structure of carbamoyl phosphate synthetase: A journey of 96 Å from substrate to product
    • Thoden J.B., Holden H.M., Wesenberg G., Raushel F.M., Rayment I. Structure of carbamoyl phosphate synthetase: a journey of 96 Å from substrate to product. Biochemistry. 36:1997;6305-6316.
    • (1997) Biochemistry , vol.36 , pp. 6305-6316
    • Thoden, J.B.1    Holden, H.M.2    Wesenberg, G.3    Raushel, F.M.4    Rayment, I.5
  • 5
    • 0028762844 scopus 로고
    • Structure of the allosteric regulatory enzyme of purine biosynthesis
    • Smith J.L., Satow Y.et al. Structure of the allosteric regulatory enzyme of purine biosynthesis. Science. 264:1994;1427-1433.
    • (1994) Science , vol.264 , pp. 1427-1433
    • Smith, J.L.1    Satow, Y.2
  • 6
    • 0029920154 scopus 로고    scopus 로고
    • Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site
    • Kim J.H., Krahn J.M., Tomchick D.R., Smith J.L., Zalkin H. Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site. J. Biol. Chem. 271:1996;15549-15557.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15549-15557
    • Kim, J.H.1    Krahn, J.M.2    Tomchick, D.R.3    Smith, J.L.4    Zalkin, H.5
  • 7
    • 0342894815 scopus 로고    scopus 로고
    • Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site
    • Krahn J.M., Kim J.H., Burns M.R., Parry R.J., Zalkin H., Smith J.L. Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site. Biochemistry. 36:1997;11061-11068.
    • (1997) Biochemistry , vol.36 , pp. 11061-11068
    • Krahn, J.M.1    Kim, J.H.2    Burns, M.R.3    Parry, R.J.4    Zalkin, H.5    Smith, J.L.6
  • 8
    • 0031941411 scopus 로고    scopus 로고
    • Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli
    • Muchmore C.R.A., Krahn J.M., Kim J.H., Zalkin H., Smith J.L. Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli. Protein Sci. 7:1998;39-51.
    • (1998) Protein Sci. , vol.7 , pp. 39-51
    • Muchmore, C.R.A.1    Krahn, J.M.2    Kim, J.H.3    Zalkin, H.4    Smith, J.L.5
  • 9
    • 0028403267 scopus 로고
    • Structure of and kinetic channelling in bifunctional dihydrofolate reductase-thymidylate synthase
    • Knighton D.R., Matthews D.A.et al. Structure of and kinetic channelling in bifunctional dihydrofolate reductase-thymidylate synthase. Nat. Struct. Biol. 1:1994;186-194.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 186-194
    • Knighton, D.R.1    Matthews, D.A.2
  • 10
    • 0028402722 scopus 로고
    • An electrostatic highway
    • Stroud R.M. An electrostatic highway. Nat. Struct. Biol. 1:1994;131-134.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 131-134
    • Stroud, R.M.1
  • 11
    • 0016588843 scopus 로고
    • Kinetic mechanism of formiminotransferase from porcine liver
    • Beaudet R., MacKenzie R.E. Kinetic mechanism of formiminotransferase from porcine liver. Biochim. Biophys. Acta. 410:1975;252-261.
    • (1975) Biochim. Biophys. Acta , vol.410 , pp. 252-261
    • Beaudet, R.1    MacKenzie, R.E.2
  • 12
    • 0019321626 scopus 로고
    • The bifunctional enzyme formiminotransferase-cyclodeaminase is a tetramer of dimers
    • MacKenzie R.E., Aldridge M., Paquin J. The bifunctional enzyme formiminotransferase-cyclodeaminase is a tetramer of dimers. J. Biol. Chem. 255:1980;9474-9478.
    • (1980) J. Biol. Chem. , vol.255 , pp. 9474-9478
    • MacKenzie, R.E.1    Aldridge, M.2    Paquin, J.3
  • 13
    • 0023647092 scopus 로고
    • Dissociation of the octameric bifunctional enzyme formiminotransferase-cyclodeaminase in urea. Isolation of two monofunctional dimers
    • Findlay W.A., MacKenzie R.E. Dissociation of the octameric bifunctional enzyme formiminotransferase-cyclodeaminase in urea. Isolation of two monofunctional dimers. Biochemistry. 26:1988;1948-1954.
    • (1988) Biochemistry , vol.26 , pp. 1948-1954
    • Findlay, W.A.1    MacKenzie, R.E.2
  • 14
    • 0029119629 scopus 로고
    • The two monofunctional domains of octameric formiminotransferase-cyclodeaminase exist as dimers
    • Murley L.L., MacKenzie R.E. The two monofunctional domains of octameric formiminotransferase-cyclodeaminase exist as dimers. Biochemistry. 34:1995;10358-10364.
    • (1995) Biochemistry , vol.34 , pp. 10358-10364
    • Murley, L.L.1    MacKenzie, R.E.2
  • 15
    • 0004590966 scopus 로고
    • R.L. Kisliuk, & G.M. Brown. Amsterdam, The Netherlands: Elsevier
    • MacKenzie R.E. Kisliuk R.L., Brown G.M. Chemistry and Biology of Pteridines. 1979;443-446 Elsevier, Amsterdam, The Netherlands.
    • (1979) Chemistry and Biology of Pteridines , pp. 443-446
    • MacKenzie, R.E.1
  • 16
    • 0018907883 scopus 로고
    • Tetrahydropteroylpolyglutamate derivatives as substrates of two multifunctional proteins with folate-dependent enzyme activities
    • MacKenzie R.E., Baugh C.M. Tetrahydropteroylpolyglutamate derivatives as substrates of two multifunctional proteins with folate-dependent enzyme activities. Biochim. Biophys. Acta. 611:1980;187-195.
    • (1980) Biochim. Biophys. Acta , vol.611 , pp. 187-195
    • MacKenzie, R.E.1    Baugh, C.M.2
  • 17
    • 0022412895 scopus 로고
    • Channeling between active sites of formiminotransferase-cyclodeaminase
    • Paquin J., Baugh C.M., MacKenzie R.E. Channeling between active sites of formiminotransferase-cyclodeaminase. J. Biol. Chem. 260:1985;14925-14931.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14925-14931
    • Paquin, J.1    Baugh, C.M.2    MacKenzie, R.E.3
  • 18
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., 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
  • 19
    • 0030902992 scopus 로고    scopus 로고
    • Monofunctional domains of formiminotransferase-cyclodeaminase retain similar conformational stabilities outside the bifunctional octamer
    • Murley L.L., MacKenzie R.E. Monofunctional domains of formiminotransferase-cyclodeaminase retain similar conformational stabilities outside the bifunctional octamer. Biochim. Biophys. Acta. 1338:1997;223-232.
    • (1997) Biochim. Biophys. Acta , vol.1338 , pp. 223-232
    • Murley, L.L.1    MacKenzie, R.E.2
  • 20
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:1991;281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 21
    • 0018796380 scopus 로고
    • Folylpolyl-gamma-glutamates as cosubstrates of 10-formyltetrahydrofolates: 5′-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase
    • Baggott J.E., Krumdieck C.L. Folylpolyl-gamma-glutamates as cosubstrates of 10-formyltetrahydrofolates: 5′-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase. Biochemistry. 18:1979;1036-1041.
    • (1979) Biochemistry , vol.18 , pp. 1036-1041
    • Baggott, J.E.1    Krumdieck, C.L.2
  • 22
    • 0033151852 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of the formiminotransferase domain from the bifunctional enzyme formiminotransferase-cyclodeaminase
    • Kohls D., Croteau N., Mejia N., MacKenzie R.E., Vrielink A. Crystallization and preliminary X-ray analysis of the formiminotransferase domain from the bifunctional enzyme formiminotransferase-cyclodeaminase. Acta Crystallogr. D. 55:1999;1206-1208.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 1206-1208
    • Kohls, D.1    Croteau, N.2    Mejia, N.3    MacKenzie, R.E.4    Vrielink, A.5
  • 25
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 26
    • 0002552477 scopus 로고
    • A yaap asap @#*? A set of averaging programs
    • E.J. Dodson, S. Gover, & W. Wolf. Warrington, UK: SERC Daresbury Laboratory
    • Jones T.A. A yaap asap @#*? A set of averaging programs. Dodson E.J., Gover S., Wolf W. Molecular Replacement. 1992;91-105 SERC Daresbury Laboratory, Warrington, UK.
    • (1992) Molecular Replacement , pp. 91-105
    • Jones, T.A.1
  • 27
    • 0031574325 scopus 로고    scopus 로고
    • Not your average density
    • Kleywegt G.J., Read R.J. Not your average density. Structure. 5:1997;1557-1569.
    • (1997) Structure , vol.5 , pp. 1557-1569
    • Kleywegt, G.J.1    Read, R.J.2
  • 28
    • 0000546402 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zhou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. D. 49:1991;18-23.
    • (1991) Acta Crystallogr. D , vol.49 , pp. 18-23
    • Jones, T.A.1    Zhou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger A.T., Kuriyan J., Karplus M. Crystallographic R factor refinement by molecular dynamics. Science. 235:1987;458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 30
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Warrem G.L. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D. 54:1998;905-921.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1    Adams, P.D.2    Clore, G.M.3    Delano, W.L.4    Gros, P.5    Warrem, G.L.6
  • 32
    • 0029011701 scopus 로고
    • A second generation force field for the simulation of proteins, nucleic acids and organic molecules
    • Cornell W.D., Kollman P.A.et al. A second generation force field for the simulation of proteins, nucleic acids and organic molecules. J. Am. Chem. Soc. 117:1995;5179-5197.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5179-5197
    • Cornell, W.D.1    Kollman, P.A.2
  • 33
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer-based archival file for macromolecular structures
    • Bernstein F.C., Tasumi M.et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112:1977;535-542.
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.C.1    Tasumi, M.2
  • 34
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 35
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans S.V. SETOR: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11:1993;134-138.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.