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Volumn 385, Issue 4, 2009, Pages 1113-1126

Unique GTP-Binding Pocket and Allostery of Uridylate Kinase from a Gram-Negative Phytopathogenic Bacterium

Author keywords

allosteric regulation; UMPK crystal structure; unique GTP binding site; Xanthomonas campestris

Indexed keywords

ADENOSINE TRIPHOSPHATE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATE; MONOMER; UNCLASSIFIED DRUG; URIDINE PHOSPHATE; URIDYLATE KINASE;

EID: 58149334786     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.11.030     Document Type: Article
Times cited : (12)

References (24)
  • 1
  • 2
    • 17644435744 scopus 로고    scopus 로고
    • Nucleoside monophosphate kinases: structure, mechanism, and substrate specificity
    • Yan H.G., and Tsai M.D. Nucleoside monophosphate kinases: structure, mechanism, and substrate specificity. Adv. Enzymol. Relat. Areas Mol. Biol. 73 (1999) 103-134
    • (1999) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.73 , pp. 103-134
    • Yan, H.G.1    Tsai, M.D.2
  • 3
    • 0037154255 scopus 로고    scopus 로고
    • A genome-scale analysis for identification of genes required for growth or survival of Haemophilus influenzae
    • Akerley B., Rubin E.J., Novick V.O., Amaya K., Judson N., and Mekalanos J.J. A genome-scale analysis for identification of genes required for growth or survival of Haemophilus influenzae. Proc. Natl Acad. Sci. USA 99 (2002) 966-971
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 966-971
    • Akerley, B.1    Rubin, E.J.2    Novick, V.O.3    Amaya, K.4    Judson, N.5    Mekalanos, J.J.6
  • 4
    • 10944266371 scopus 로고    scopus 로고
    • UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
    • Fassy F., Krebs O., Lowinski M., Ferrari P., Winter J., Collard-Dutilleul V., and Hocini K.S. UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation. Biochem. J. 384 (2004) 619-627
    • (2004) Biochem. J. , vol.384 , pp. 619-627
    • Fassy, F.1    Krebs, O.2    Lowinski, M.3    Ferrari, P.4    Winter, J.5    Collard-Dutilleul, V.6    Hocini, K.S.7
  • 5
    • 0028953772 scopus 로고
    • Escherichia coli UMP-kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP
    • Serina L., Blondin C., Krin E., Sismerio O., Danchih A., Sakamoto H., et al. Escherichia coli UMP-kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP. Biochemistry 34 (1995) 5066-5074
    • (1995) Biochemistry , vol.34 , pp. 5066-5074
    • Serina, L.1    Blondin, C.2    Krin, E.3    Sismerio, O.4    Danchih, A.5    Sakamoto, H.6
  • 6
    • 77956943185 scopus 로고
    • Nucleoside and nucleotide kinases
    • Boyer P.D. (Ed), Academic Press, New York, NY
    • Anderson E.P. Nucleoside and nucleotide kinases. In: Boyer P.D. (Ed). The Enzymes. 3rd edit Vol. 8 (1973), Academic Press, New York, NY 49-96
    • (1973) The Enzymes. 3rd edit , vol.8 , pp. 49-96
    • Anderson, E.P.1
  • 7
    • 0034595434 scopus 로고    scopus 로고
    • The 1.5 Å resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases
    • Ramon-Maiques S., Marina A., Uriarte M., Fita I., and Rubio V. The 1.5 Å resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases. J. Mol. Biol. 299 (2000) 463-476
    • (2000) J. Mol. Biol. , vol.299 , pp. 463-476
    • Ramon-Maiques, S.1    Marina, A.2    Uriarte, M.3    Fita, I.4    Rubio, V.5
  • 8
    • 23944435947 scopus 로고    scopus 로고
    • The crystal structure of Pyrococcus furiosus UMP kinase provides insight into catalysis and regulation in microbial pyrimidine nucleotide biosynthesis
    • Marco-Marin C., Gil-Ortiz F., and Rubio V. The crystal structure of Pyrococcus furiosus UMP kinase provides insight into catalysis and regulation in microbial pyrimidine nucleotide biosynthesis. J. Mol. Biol. 352 (2005) 438-454
    • (2005) J. Mol. Biol. , vol.352 , pp. 438-454
    • Marco-Marin, C.1    Gil-Ortiz, F.2    Rubio, V.3
  • 9
    • 0036118398 scopus 로고    scopus 로고
    • Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family during catalysis
    • Ramon-Maiques S., Marina A., Gil-Ortiz F., Fita I., and Rubio V. Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family during catalysis. Structure 10 (2002) 329-342
    • (2002) Structure , vol.10 , pp. 329-342
    • Ramon-Maiques, S.1    Marina, A.2    Gil-Ortiz, F.3    Fita, I.4    Rubio, V.5
  • 10
    • 0032950478 scopus 로고    scopus 로고
    • Carbamate kinase: new structural machinery for making carbamoyl phosphate, the common precursor of pyrimidines and arginine
    • Marina A., Alzari P.M., Bravo J., Uriarte M., Bacrcelona B., Fita I., and Rubio V. Carbamate kinase: new structural machinery for making carbamoyl phosphate, the common precursor of pyrimidines and arginine. Protein Sci. 8 (1999) 934-940
    • (1999) Protein Sci. , vol.8 , pp. 934-940
    • Marina, A.1    Alzari, P.M.2    Bravo, J.3    Uriarte, M.4    Bacrcelona, B.5    Fita, I.6    Rubio, V.7
  • 11
    • 34147149525 scopus 로고    scopus 로고
    • Regulatory mechanisms differ in UMP kinases from Gram-negative and Gram-positive bacteria
    • Evrin C., Straut M., Slavova-Azmanova N., Bucuernci N., Onu A., Assairi L., et al. Regulatory mechanisms differ in UMP kinases from Gram-negative and Gram-positive bacteria. J. Biol. Chem. 282 (2007) 7242-7253
    • (2007) J. Biol. Chem. , vol.282 , pp. 7242-7253
    • Evrin, C.1    Straut, M.2    Slavova-Azmanova, N.3    Bucuernci, N.4    Onu, A.5    Assairi, L.6
  • 12
    • 0043270606 scopus 로고    scopus 로고
    • UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal activity
    • Gagyi C., Bucurenci N., Sirbu O., Labesse G., Ionescu M., Ofiteru A., et al. UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal activity. Eur. J. Biochem. 270 (2003) 3196-3204
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3196-3204
    • Gagyi, C.1    Bucurenci, N.2    Sirbu, O.3    Labesse, G.4    Ionescu, M.5    Ofiteru, A.6
  • 13
    • 33947221897 scopus 로고    scopus 로고
    • Structural and enzymatic investigation of the Sulfolobus solfataricus uridylate kinase shows competitive UTP inhibition and the lack of GTP stimulation
    • Jensen K.S., Johansson E., and Jensen K.F. Structural and enzymatic investigation of the Sulfolobus solfataricus uridylate kinase shows competitive UTP inhibition and the lack of GTP stimulation. Biochemistry 46 (2007) 2745-2757
    • (2007) Biochemistry , vol.46 , pp. 2745-2757
    • Jensen, K.S.1    Johansson, E.2    Jensen, K.F.3
  • 14
    • 36749044833 scopus 로고    scopus 로고
    • Structural and functional investigations of Ureaplasma parvum UMP kinase-a potential antibacterial drug target
    • Egeblad-Welin L., Welin M., Wang L., and Eriksson S. Structural and functional investigations of Ureaplasma parvum UMP kinase-a potential antibacterial drug target. FEBS J. 274 (2007) 6403-6414
    • (2007) FEBS J. , vol.274 , pp. 6403-6414
    • Egeblad-Welin, L.1    Welin, M.2    Wang, L.3    Eriksson, S.4
  • 15
    • 21844477035 scopus 로고    scopus 로고
    • Structure of Escherichia coli UPM kinase differs from that of other nucleoside monophosphate kinases and sheds new light on enzyme regulation
    • Briozzo P., Evrin C., Meyer P., Assairi L., Joly N., Barzu O., and Gilles A.-M. Structure of Escherichia coli UPM kinase differs from that of other nucleoside monophosphate kinases and sheds new light on enzyme regulation. J. Biol. Chem. 280 (2005) 25533-25540
    • (2005) J. Biol. Chem. , vol.280 , pp. 25533-25540
    • Briozzo, P.1    Evrin, C.2    Meyer, P.3    Assairi, L.4    Joly, N.5    Barzu, O.6    Gilles, A.-M.7
  • 16
    • 48749129111 scopus 로고    scopus 로고
    • The crystal structure of UMP kinase from Bacillus anthracis (BA1797) reveals an allosteric nucleotide-binding site
    • Meier C., Carter L.G., Sanisbury S., Mancini E.J., Owens R.J., Stuart D.I., and Esnouf R.M. The crystal structure of UMP kinase from Bacillus anthracis (BA1797) reveals an allosteric nucleotide-binding site. J. Mol. Biol. 381 (2008) 1098-1105
    • (2008) J. Mol. Biol. , vol.381 , pp. 1098-1105
    • Meier, C.1    Carter, L.G.2    Sanisbury, S.3    Mancini, E.J.4    Owens, R.J.5    Stuart, D.I.6    Esnouf, R.M.7
  • 17
    • 34248144327 scopus 로고    scopus 로고
    • The crystallization of apo-form UMP kinase from Xanthomonas campestris is significantly improved in a strong magnetic field
    • Tu J.-L., Chin K.-H., Wang A.H.-J., and Chou S.-H. The crystallization of apo-form UMP kinase from Xanthomonas campestris is significantly improved in a strong magnetic field. Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. 63 (2007) 438-442
    • (2007) Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. , vol.63 , pp. 438-442
    • Tu, J.-L.1    Chin, K.-H.2    Wang, A.H.-J.3    Chou, S.-H.4
  • 19
    • 24044526890 scopus 로고    scopus 로고
    • Structural consequences of hen egg-white lysozyme orthorhombic crystal growth in a high magnetic field: validation of X-ray diffraction intensity, conformational energy searching and quantitative analysis of B factors and mosaicity
    • Saijo S., Yamada Y., Sato T., Tanaka N., Matsui T., Sazaki G., et al. Structural consequences of hen egg-white lysozyme orthorhombic crystal growth in a high magnetic field: validation of X-ray diffraction intensity, conformational energy searching and quantitative analysis of B factors and mosaicity. Acta Crystallogr., Sect. D: Biol. Crystallogr. 61 (2005) 207-217
    • (2005) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.61 , pp. 207-217
    • Saijo, S.1    Yamada, Y.2    Sato, T.3    Tanaka, N.4    Matsui, T.5    Sazaki, G.6
  • 20
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • Aslanidis C., and de Jong P.J. Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res. 18 (1990) 6069-6074
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6069-6074
    • Aslanidis, C.1    de Jong, P.J.2
  • 21
    • 0031059866 scopus 로고    scopus 로고
    • Processing of the X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of the 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
  • 24
    • 0028291887 scopus 로고
    • Improved spectrophotometric assay of nucleoside monophosphate kinase activity using the pyruvate kinase/lactate dehydrogenase coupling system
    • Blondin C., Serina L., Wiesmüller L., Gilles A.M., and Bârzu O. Improved spectrophotometric assay of nucleoside monophosphate kinase activity using the pyruvate kinase/lactate dehydrogenase coupling system. Anal. Biochem. 220 (1994) 219-221
    • (1994) Anal. Biochem. , vol.220 , pp. 219-221
    • Blondin, C.1    Serina, L.2    Wiesmüller, L.3    Gilles, A.M.4    Bârzu, O.5


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