메뉴 건너뛰기




Volumn 14, Issue 8, 2006, Pages 1251-1261

Prokaryotic Type II and Type III Pantothenate Kinases: The Same Monomer Fold Creates Dimers with Distinct Catalytic Properties

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENINE NUCLEOTIDE; ADENOSINE TRIPHOSPHATE; ANTIBIOTIC AGENT; COENZYME A; DIMER; ISOENZYME; MONOMER; MONOVALENT CATION; PANTOTHENATE KINASE; PANTOTHENIC ACID;

EID: 33746822335     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2006.06.008     Document Type: Article
Times cited : (53)

References (52)
  • 1
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork P., Sander C., and Valencia A. An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc. Natl. Acad. Sci. USA 89 (1992) 7290-7294
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 2
    • 20144366768 scopus 로고    scopus 로고
    • Characterization of a new pantothenate kinase isoform from Helicobacter pylori
    • Brand L.A., and Strauss E. Characterization of a new pantothenate kinase isoform from Helicobacter pylori. J. Biol. Chem. 280 (2005) 20185-20188
    • (2005) J. Biol. Chem. , vol.280 , pp. 20185-20188
    • Brand, L.A.1    Strauss, E.2
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4 (Collaborative Computation Project, Number 4)
    • CCP4 (Collaborative Computation Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 6
    • 0036305943 scopus 로고    scopus 로고
    • Sequence and structure classification of kinases
    • Cheek S., Zhang H., and Grishin N.V. Sequence and structure classification of kinases. J. Mol. Biol. 320 (2002) 855-881
    • (2002) J. Mol. Biol. , vol.320 , pp. 855-881
    • Cheek, S.1    Zhang, H.2    Grishin, N.V.3
  • 7
    • 17844401480 scopus 로고    scopus 로고
    • A comprehensive update of the sequence and structure classification of kinases
    • Cheek S., Ginalski K., Zhang H., and Grishin N.V. A comprehensive update of the sequence and structure classification of kinases. BMC Struct. Biol. 5 (2005) 6
    • (2005) BMC Struct. Biol. , vol.5 , pp. 6
    • Cheek, S.1    Ginalski, K.2    Zhang, H.3    Grishin, N.V.4
  • 8
    • 0029620544 scopus 로고
    • Mechanisms of phosphoryl and acyl transfer
    • Cleland W.W., and Hengge A.C. Mechanisms of phosphoryl and acyl transfer. FASEB J. 9 (1995) 1585-1594
    • (1995) FASEB J. , vol.9 , pp. 1585-1594
    • Cleland, W.W.1    Hengge, A.C.2
  • 9
    • 0032489438 scopus 로고    scopus 로고
    • Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus. Purification and characterization of the native enzyme
    • delCardayre S.B., Stock K.P., Newton G.L., Fahey R.C., and Davies J.E. Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus. Purification and characterization of the native enzyme. J. Biol. Chem. 273 (1998) 5744-5751
    • (1998) J. Biol. Chem. , vol.273 , pp. 5744-5751
    • delCardayre, S.B.1    Stock, K.P.2    Newton, G.L.3    Fahey, R.C.4    Davies, J.E.5
  • 10
    • 33644686444 scopus 로고    scopus 로고
    • Enzymes activated by monovalent cations: a structural perspective
    • Di Cera E. Enzymes activated by monovalent cations: a structural perspective. J. Biol. Chem. 281 (2006) 1305-1308
    • (2006) J. Biol. Chem. , vol.281 , pp. 1305-1308
    • Di Cera, E.1
  • 11
    • 0035158003 scopus 로고    scopus 로고
    • Thermotoga maritima phosphofructokinases: expression and characterization of two unique enzymes
    • Ding Y.R., Ronimus R.S., and Morgan H.W. Thermotoga maritima phosphofructokinases: expression and characterization of two unique enzymes. J. Bacteriol. 183 (2001) 791-794
    • (2001) J. Bacteriol. , vol.183 , pp. 791-794
    • Ding, Y.R.1    Ronimus, R.S.2    Morgan, H.W.3
  • 12
    • 0037322485 scopus 로고    scopus 로고
    • An isoform of hPANK2, deficient in pantothenate kinase-associated neurodegeneration, localizes to mitochondria
    • Hörtnagel K., Prokisch H., and Meitinger T. An isoform of hPANK2, deficient in pantothenate kinase-associated neurodegeneration, localizes to mitochondria. Hum. Mol. Genet. 12 (2003) 321-327
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 321-327
    • Hörtnagel, K.1    Prokisch, H.2    Meitinger, T.3
  • 13
    • 4143098353 scopus 로고    scopus 로고
    • The structure of the pantothenate kinase-ADP-pantothenate ternary complex reveals the relationship between the binding sites for substrate, allosteric regulator and antimetabolites
    • Ivey R.A., Zhang Y.-M., Virga K.G., Hevener K., Lee R.E., Rock C.O., Jackowski S., and Park H.-W. The structure of the pantothenate kinase-ADP-pantothenate ternary complex reveals the relationship between the binding sites for substrate, allosteric regulator and antimetabolites. J. Biol. Chem. 279 (2004) 35622-35629
    • (2004) J. Biol. Chem. , vol.279 , pp. 35622-35629
    • Ivey, R.A.1    Zhang, Y.-M.2    Virga, K.G.3    Hevener, K.4    Lee, R.E.5    Rock, C.O.6    Jackowski, S.7    Park, H.-W.8
  • 14
    • 27944436648 scopus 로고    scopus 로고
    • Structural basis of interdomain communication in the Hsc70 chaperone
    • Jiang J., Prasad K., Lafer E.M., and Sousa R. Structural basis of interdomain communication in the Hsc70 chaperone. Mol. Cell 20 (2005) 513-524
    • (2005) Mol. Cell , vol.20 , pp. 513-524
    • Jiang, J.1    Prasad, K.2    Lafer, E.M.3    Sousa, R.4
  • 15
    • 0033578346 scopus 로고    scopus 로고
    • Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein
    • Johnson E.R., and McKay D.B. Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein. Biochemistry 38 (1999) 10823-10830
    • (1999) Biochemistry , vol.38 , pp. 10823-10830
    • Johnson, E.R.1    McKay, D.B.2
  • 16
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 17
    • 0028944687 scopus 로고
    • The actin fold
    • Kabsch W., and Holmes K.C. The actin fold. FASEB J. 9 (1995) 167-174
    • (1995) FASEB J. , vol.9 , pp. 167-174
    • Kabsch, W.1    Holmes, K.C.2
  • 18
    • 84908717757 scopus 로고
    • Kinetic analysis of enzyme reactions. II. The potassium activation and calcium inhibition of pyruvic phosphoferase
    • Kachmer J.F., and Boyer P.D. Kinetic analysis of enzyme reactions. II. The potassium activation and calcium inhibition of pyruvic phosphoferase. J. Biol. Chem. 200 (1953) 669-682
    • (1953) J. Biol. Chem. , vol.200 , pp. 669-682
    • Kachmer, J.F.1    Boyer, P.D.2
  • 19
    • 19644383169 scopus 로고    scopus 로고
    • Hypothesis: structures, evolution, and ancestor of glucose kinases in the hexokinase family
    • Kawai S., Mukai T., Mori S., Mikami B., and Murata K. Hypothesis: structures, evolution, and ancestor of glucose kinases in the hexokinase family. J. Biosci. Bioeng. 99 (2005) 320-330
    • (2005) J. Biosci. Bioeng. , vol.99 , pp. 320-330
    • Kawai, S.1    Mukai, T.2    Mori, S.3    Mikami, B.4    Murata, K.5
  • 20
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. 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.J.1
  • 22
    • 13544275017 scopus 로고    scopus 로고
    • A pantothenate kinase from Staphylococcus aureus refractory to feedback regulation by coenzyme A
    • Leonardi R., Chohnan S., Zhang Y.-M., Virga K.G., Lee R.E., Rock C.O., and Jackowski S. A pantothenate kinase from Staphylococcus aureus refractory to feedback regulation by coenzyme A. J. Biol. Chem. 280 (2005) 3314-3322
    • (2005) J. Biol. Chem. , vol.280 , pp. 3314-3322
    • Leonardi, R.1    Chohnan, S.2    Zhang, Y.-M.3    Virga, K.G.4    Lee, R.E.5    Rock, C.O.6    Jackowski, S.7
  • 24
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. 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
  • 25
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: photorealistic molecular graphics
    • Merritt E.A., and Bacon D.J. 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
  • 26
    • 0030724727 scopus 로고    scopus 로고
    • Mechanisms of signaling and related enzymes
    • Mildvan A.S. Mechanisms of signaling and related enzymes. Proteins 29 (1997) 401-416
    • (1997) Proteins , vol.29 , pp. 401-416
    • Mildvan, A.S.1
  • 29
    • 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
  • 31
    • 0033954772 scopus 로고    scopus 로고
    • Pantothenate kinase regulation of the intracellular concentration of coenzyme A
    • Rock C.O., Calder R.B., Karim M.A., and Jackowski S. Pantothenate kinase regulation of the intracellular concentration of coenzyme A. J. Biol. Chem. 275 (2000) 1377-1383
    • (2000) J. Biol. Chem. , vol.275 , pp. 1377-1383
    • Rock, C.O.1    Calder, R.B.2    Karim, M.A.3    Jackowski, S.4
  • 32
    • 0037193667 scopus 로고    scopus 로고
    • The murine Pank1 gene encodes two differentially regulated pantothenate kinase isozymes
    • Rock C.O., Karim M.A., Zhang Y.-M., and Jackowski S. The murine Pank1 gene encodes two differentially regulated pantothenate kinase isozymes. Gene 291 (2002) 35-43
    • (2002) Gene , vol.291 , pp. 35-43
    • Rock, C.O.1    Karim, M.A.2    Zhang, Y.-M.3    Jackowski, S.4
  • 33
    • 0037853313 scopus 로고    scopus 로고
    • Role of feedback regulation of pantothenate kinase (CoaA) in the control of coenzyme A levels in Escherichia coli
    • Rock C.O., Park H.-W., and Jackowski S. Role of feedback regulation of pantothenate kinase (CoaA) in the control of coenzyme A levels in Escherichia coli. J. Bacteriol. 185 (2003) 3410-3415
    • (2003) J. Bacteriol. , vol.185 , pp. 3410-3415
    • Rock, C.O.1    Park, H.-W.2    Jackowski, S.3
  • 34
    • 0026778799 scopus 로고
    • Cloning, sequencing, and expression of the pantothenate kinase (coaA) gene of Escherichia coli
    • Song W.-J., and Jackowski S. Cloning, sequencing, and expression of the pantothenate kinase (coaA) gene of Escherichia coli. J. Bacteriol. 174 (1992) 6411-6417
    • (1992) J. Bacteriol. , vol.174 , pp. 6411-6417
    • Song, W.-J.1    Jackowski, S.2
  • 35
    • 0028104163 scopus 로고
    • Kinetics and regulation of pantothenate kinase from Escherichia coli
    • Song W.-J., and Jackowski S. Kinetics and regulation of pantothenate kinase from Escherichia coli. J. Biol. Chem. 269 (1994) 27051-27058
    • (1994) J. Biol. Chem. , vol.269 , pp. 27051-27058
    • Song, W.-J.1    Jackowski, S.2
  • 36
    • 0037073693 scopus 로고    scopus 로고
    • The antibiotic activity of N-pentylpantothenamide results from its conversion to ethyldethia-coenzyme A, a coenzyme A antimetabolite
    • Strauss E., and Begley T.P. The antibiotic activity of N-pentylpantothenamide results from its conversion to ethyldethia-coenzyme A, a coenzyme A antimetabolite. J. Biol. Chem. 277 (2002) 48205-48209
    • (2002) J. Biol. Chem. , vol.277 , pp. 48205-48209
    • Strauss, E.1    Begley, T.P.2
  • 37
    • 0040566017 scopus 로고
    • Monovalent cations in enzyme-catalyzed reactions
    • Sigel H. (Ed), Marcel Dekker, Inc., New York
    • Suelter C.H. Monovalent cations in enzyme-catalyzed reactions. In: Sigel H. (Ed). High Molecular Complexes (1974), Marcel Dekker, Inc., New York 201-251
    • (1974) High Molecular Complexes , pp. 201-251
    • Suelter, C.H.1
  • 38
    • 0041835984 scopus 로고    scopus 로고
    • Strictly polyphosphate-dependent glucokinase in a polyphosphate-accumulating bacterium, Microlunatus phosphovorus
    • Tanaka S., Lee S.O., Hamaoka K., Kato J., Takiguchi N., Nakamura K., Ohtake H., and Kuroda A. Strictly polyphosphate-dependent glucokinase in a polyphosphate-accumulating bacterium, Microlunatus phosphovorus. J. Bacteriol. 185 (2003) 5654-5656
    • (2003) J. Bacteriol. , vol.185 , pp. 5654-5656
    • Tanaka, S.1    Lee, S.O.2    Hamaoka, K.3    Kato, J.4    Takiguchi, N.5    Nakamura, K.6    Ohtake, H.7    Kuroda, A.8
  • 41
    • 0023608181 scopus 로고
    • Isolation and characterization of temperature-sensitive pantothenate kinase (coaA) mutants of Escherichia coli
    • Vallari D.S., and Rock C.O. Isolation and characterization of temperature-sensitive pantothenate kinase (coaA) mutants of Escherichia coli. J. Bacteriol. 169 (1987) 5795-5800
    • (1987) J. Bacteriol. , vol.169 , pp. 5795-5800
    • Vallari, D.S.1    Rock, C.O.2
  • 42
    • 0023664065 scopus 로고
    • Regulation of pantothenate kinase by coenzyme A and its thioesters
    • Vallari D.S., Jackowski S., and Rock C.O. Regulation of pantothenate kinase by coenzyme A and its thioesters. J. Biol. Chem. 262 (1987) 2468-2471
    • (1987) J. Biol. Chem. , vol.262 , pp. 2468-2471
    • Vallari, D.S.1    Jackowski, S.2    Rock, C.O.3
  • 44
    • 0028172499 scopus 로고
    • Construction of improved Escherichia-Pseudomonas shuttle vectors derived from pUC18/19 and sequence of the region required for their replication in Pseudomonas aeruginosa
    • West S.E., Schweizer H.P., Dall C., Sample A.K., and Runyen-Janecky L.J. Construction of improved Escherichia-Pseudomonas shuttle vectors derived from pUC18/19 and sequence of the region required for their replication in Pseudomonas aeruginosa. Gene 148 (1994) 81-86
    • (1994) Gene , vol.148 , pp. 81-86
    • West, S.E.1    Schweizer, H.P.2    Dall, C.3    Sample, A.K.4    Runyen-Janecky, L.J.5
  • 45
    • 0028938819 scopus 로고
    • How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site
    • Wilbanks S.M., and McKay D.B. How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site. J. Biol. Chem. 270 (1995) 2251-2257
    • (1995) J. Biol. Chem. , vol.270 , pp. 2251-2257
    • Wilbanks, S.M.1    McKay, D.B.2
  • 46
    • 0028287525 scopus 로고
    • Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants
    • Wilbanks S.M., Luca-Flaherty C., and McKay D.B. Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants. J. Biol. Chem. 269 (1994) 12893-12898
    • (1994) J. Biol. Chem. , vol.269 , pp. 12893-12898
    • Wilbanks, S.M.1    Luca-Flaherty, C.2    McKay, D.B.3
  • 47
    • 33746838839 scopus 로고    scopus 로고
    • Yocum, R.R., and Patterson, T.A. November 2004. U.S. patent 6,830,898.
  • 48
    • 0034623086 scopus 로고    scopus 로고
    • Structural basis for the feedback regulation of Eschericia coli pantothenate kinase by coenzyme A
    • Yun M., Park C.-G., Kim J.-Y., Rock C.O., Jackowski S., and Park H.-W. Structural basis for the feedback regulation of Eschericia coli pantothenate kinase by coenzyme A. J. Biol. Chem. 275 (2000) 28093-28099
    • (2000) J. Biol. Chem. , vol.275 , pp. 28093-28099
    • Yun, M.1    Park, C.-G.2    Kim, J.-Y.3    Rock, C.O.4    Jackowski, S.5    Park, H.-W.6
  • 49
    • 10944262320 scopus 로고    scopus 로고
    • Acyl carrier protein is a cellular target for the antibacterial action of the pantothenamide class of pantothenate antimetabolites
    • Zhang Y.-M., Frank M.W., Virga K.G., Lee R.E., Rock C.O., and Jackowski S. Acyl carrier protein is a cellular target for the antibacterial action of the pantothenamide class of pantothenate antimetabolites. J. Biol. Chem. 279 (2004) 50969-50975
    • (2004) J. Biol. Chem. , vol.279 , pp. 50969-50975
    • Zhang, Y.-M.1    Frank, M.W.2    Virga, K.G.3    Lee, R.E.4    Rock, C.O.5    Jackowski, S.6
  • 50
    • 25444432519 scopus 로고    scopus 로고
    • Feedback regulation of murine pantothenate kinase 3 by coenzyme A and coenzyme A thioesters
    • Zhang Y.-M., Rock C.O., and Jackowski S. Feedback regulation of murine pantothenate kinase 3 by coenzyme A and coenzyme A thioesters. J. Biol. Chem. 280 (2005) 32594-32601
    • (2005) J. Biol. Chem. , vol.280 , pp. 32594-32601
    • Zhang, Y.-M.1    Rock, C.O.2    Jackowski, S.3
  • 51
    • 33644864274 scopus 로고    scopus 로고
    • Biochemical properties of human pantothenate kinase 2 isoforms and mutations linked to pantothenate kinase-associated neurodegeneration
    • Zhang Y.-M., Rock C.O., and Jackowski S. Biochemical properties of human pantothenate kinase 2 isoforms and mutations linked to pantothenate kinase-associated neurodegeneration. J. Biol. Chem. 281 (2006) 107-114
    • (2006) J. Biol. Chem. , vol.281 , pp. 107-114
    • Zhang, Y.-M.1    Rock, C.O.2    Jackowski, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.