메뉴 건너뛰기




Volumn 12, Issue 11, 2004, Pages 1947-1954

An alternate conformation and a third metal in PstP/Ppp, the M. tuberculosis PP2C-family Ser/Thr protein phosphatase

Author keywords

[No Author keywords available]

Indexed keywords

4 NITROPHENYL PHOSPHATE; MANGANESE; PROTEIN SERINE THREONINE KINASE;

EID: 7944221188     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2004.09.008     Document Type: Article
Times cited : (89)

References (34)
  • 1
    • 0034194181 scopus 로고    scopus 로고
    • The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis
    • Av-Gay Y., Everett M. The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis. Trends Microbiol. 8:2000;238-244
    • (2000) Trends Microbiol. , vol.8 , pp. 238-244
    • Av-Gay, Y.1    Everett, M.2
  • 2
    • 0032728879 scopus 로고    scopus 로고
    • Expression and characterization of the Mycobacterium tuberculosis serine/threonine protein kinase PknB
    • Av-Gay Y., Jamil S., Drews S.J. Expression and characterization of the Mycobacterium tuberculosis serine/threonine protein kinase PknB. Infect. Immun. 67:1999;5676-5682
    • (1999) Infect. Immun. , vol.67 , pp. 5676-5682
    • Av-Gay, Y.1    Jamil, S.2    Drews, S.J.3
  • 3
    • 0031860103 scopus 로고    scopus 로고
    • The structure and mechanism of protein phosphatases: Insights into catalysis and regulation
    • Barford D., Das A.K., Egloff M.P. The structure and mechanism of protein phosphatases. insights into catalysis and regulation Annu. Rev. Biophys. Biomol. Struct. 27:1998;133-164
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 133-164
    • Barford, D.1    Das, A.K.2    Egloff, M.P.3
  • 4
    • 0038805137 scopus 로고    scopus 로고
    • Susceptibility to mycobacterial infections: The importance of host genetics
    • Bellamy R. Susceptibility to mycobacterial infections. the importance of host genetics Genes Immun. 4:2003;4-11
    • (2003) Genes Immun. , vol.4 , pp. 4-11
    • Bellamy, R.1
  • 5
    • 0141454865 scopus 로고    scopus 로고
    • PknB kinase activity is regulated by phosphorylation in two Thr residues and dephosphorylation by PstP, the cognate phospho-Ser/Thr phosphatase, in Mycobacterium tuberculosis
    • Boitel B., Ortiz-Lombardia M., Duran R., Pompeo F., Cole S.T., Cervenansky C., Alzari P.M. PknB kinase activity is regulated by phosphorylation in two Thr residues and dephosphorylation by PstP, the cognate phospho-Ser/Thr phosphatase, in Mycobacterium tuberculosis. Mol. Microbiol. 49:2003;1493-1508
    • (2003) Mol. Microbiol. , vol.49 , pp. 1493-1508
    • Boitel, B.1    Ortiz-Lombardia, M.2    Duran, R.3    Pompeo, F.4    Cole, S.T.5    Cervenansky, C.6    Alzari, P.M.7
  • 6
    • 1442335020 scopus 로고    scopus 로고
    • A genome-wide survey of human tyrosine phosphatases
    • Bhaduri A., Sowdhamini R. A genome-wide survey of human tyrosine phosphatases. Protein Eng. 16:2003;881-888
    • (2003) Protein Eng. , vol.16 , pp. 881-888
    • Bhaduri, A.1    Sowdhamini, R.2
  • 7
    • 0036183002 scopus 로고    scopus 로고
    • Evidence that a eukaryotic-type serine/threonine protein kinase from Mycobacterium tuberculosis regulates morphological changes associated with cell division
    • Chaba R., Raje M., Chakraborti P.K. Evidence that a eukaryotic-type serine/threonine protein kinase from Mycobacterium tuberculosis regulates morphological changes associated with cell division. Eur. J. Biochem. 269:2002;1078-1085
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1078-1085
    • Chaba, R.1    Raje, M.2    Chakraborti, P.K.3
  • 10
    • 0030465532 scopus 로고    scopus 로고
    • Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 a resolution
    • Das A.K., Helps N.R., Cohen P.T., Barford D. Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution. EMBO J. 15:1996;6798-6809
    • (1996) EMBO J. , vol.15 , pp. 6798-6809
    • Das, A.K.1    Helps, N.R.2    Cohen, P.T.3    Barford, D.4
  • 11
    • 0033575250 scopus 로고    scopus 로고
    • Kinetic analysis of human serine/threonine protein phosphatase 2Cα
    • Fjeld C.C., Denu J.M. Kinetic analysis of human serine/threonine protein phosphatase 2Cα J. Biol. Chem. 274:1999;20336-20343
    • (1999) J. Biol. Chem. , vol.274 , pp. 20336-20343
    • Fjeld, C.C.1    Denu, J.M.2
  • 12
    • 0042952817 scopus 로고    scopus 로고
    • The global transcriptional response of Bacillus subtilis to manganese involves the MntR, Fur, TnrA and sigmaB regulons
    • Guedon E., Moore C.M., Que Q., Wang T., Ye R.W., Helmann J.D. The global transcriptional response of Bacillus subtilis to manganese involves the MntR, Fur, TnrA and sigmaB regulons. Mol. Microbiol. 49:2003;1477-1491
    • (2003) Mol. Microbiol. , vol.49 , pp. 1477-1491
    • Guedon, E.1    Moore, C.M.2    Que, Q.3    Wang, T.4    Ye, R.W.5    Helmann, J.D.6
  • 13
    • 1242274650 scopus 로고    scopus 로고
    • Automated protein crystal structure determination using Elves
    • Holton J.M., Alber T. Automated protein crystal structure determination using Elves. Proc. Natl. Acad. Sci. USA. 101:2004;1537-1542
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1537-1542
    • Holton, J.M.1    Alber, T.2
  • 14
    • 0035413604 scopus 로고    scopus 로고
    • Molecular reactions of protein phosphatases-insights from structure and chemistry
    • Jackson M.D., Denu J.M. Molecular reactions of protein phosphatases-insights from structure and chemistry. Chem. Rev. 10:2001;2313-2340
    • (2001) Chem. Rev. , vol.10 , pp. 2313-2340
    • Jackson, M.D.1    Denu, J.M.2
  • 15
    • 0037779029 scopus 로고    scopus 로고
    • Probing the function of conserved residues in the serine/threonine phosphatase PP2Cα
    • Jackson M.D., Fjeld C.C., Denu J.M. Probing the function of conserved residues in the serine/threonine phosphatase PP2Cα Biochemistry. 42:2003;8513-8521
    • (2003) Biochemistry , vol.42 , pp. 8513-8521
    • Jackson, M.D.1    Fjeld, C.C.2    Denu, J.M.3
  • 16
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou 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. A47:1991;110-119
    • (1991) Acta Crystallogr. , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 17
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley L.A., MacCallum R.M., Sternberg M.J. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J. Mol. Biol. 299:2000;499-520
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 18
    • 0037005989 scopus 로고    scopus 로고
    • Protein kinases and protein phosphatases in prokaryotes: A genomic perspective
    • Kennelly P.J. Protein kinases and protein phosphatases in prokaryotes. a genomic perspective FEMS Microbiol. Lett. 206:2002;1-8
    • (2002) FEMS Microbiol. Lett. , vol.206 , pp. 1-8
    • Kennelly, P.J.1
  • 19
    • 0035983678 scopus 로고    scopus 로고
    • The complement of protein phosphatase catalytic subunits encoded in the genome of Arabidopsis
    • Kerk D., Bulgrien J., Smith D.W., Barsam B., Veretnik S., Gribskov M. The complement of protein phosphatase catalytic subunits encoded in the genome of Arabidopsis. Plant Physiol. 129:2002;908-925
    • (2002) Plant Physiol. , vol.129 , pp. 908-925
    • Kerk, D.1    Bulgrien, J.2    Smith, D.W.3    Barsam, B.4    Veretnik, S.5    Gribskov, M.6
  • 20
    • 0034873897 scopus 로고    scopus 로고
    • Serine/threonine protein kinases PknF and PknG of Mycobacterium tuberculosis: Characterization and localization
    • Koul A., Choidas A., Tyagi A.K., Drlica K., Singh Y., Ullrich A. Serine/threonine protein kinases PknF and PknG of Mycobacterium tuberculosis. characterization and localization Microbiology. 147:2001;2307-2314
    • (2001) Microbiology , vol.147 , pp. 2307-2314
    • Koul, A.1    Choidas, A.2    Tyagi, A.K.3    Drlica, K.4    Singh, Y.5    Ullrich, A.6
  • 22
    • 0034644524 scopus 로고    scopus 로고
    • Conservation and innovation in plant signaling pathways
    • McCarty D.R., Chory J. Conservation and innovation in plant signaling pathways. Cell. 103:2000;201-209
    • (2000) Cell , vol.103 , pp. 201-209
    • McCarty, D.R.1    Chory, J.2
  • 23
    • 0348223992 scopus 로고    scopus 로고
    • An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis
    • Molle V., Kremer L., Girard-Blanc C., Besra G.S., Cozzone A.J., Prost J.F. An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis. Biochemistry. 42:2003;15300-15309
    • (2003) Biochemistry , vol.42 , pp. 15300-15309
    • Molle, V.1    Kremer, L.2    Girard-Blanc, C.3    Besra, G.S.4    Cozzone, A.J.5    Prost, J.F.6
  • 24
    • 0036077402 scopus 로고    scopus 로고
    • ARP/wARP's model-building algorithms. I. the main chain
    • Morris R.J., Perrakis A., Lamzin V.S. ARP/wARP's model-building algorithms. I. The main chain. Acta Crystallogr. D58:2002;968-975
    • (2002) Acta Crystallogr. , vol.58 , pp. 968-975
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 25
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D53:1997;240-255
    • (1997) Acta Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • C.W. Jr. Carter, & R. Sweet. New York: Academic Press
    • Otwinowski Z., Minor W. Processing of x-ray diffraction data collected in oscillation mode. Carter C.W. Jr., Sweet R. Methods in Enzymology, Volume 276. 1997;307-326 Academic Press, New York
    • (1997) Methods in Enzymology, Volume 276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 0031828101 scopus 로고    scopus 로고
    • Sticky-end PCR: New method for subcloning
    • Pham K., LaForge K.S., Kreek M.J. Sticky-end PCR. new method for subcloning Biotechniques. 25:1998;206-208
    • (1998) Biotechniques , vol.25 , pp. 206-208
    • Pham, K.1    Laforge, K.S.2    Kreek, M.J.3
  • 29
    • 0035432383 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis: Here today, and here tomorrow
    • Russell D.G. Mycobacterium tuberculosis. here today, and here tomorrow Nat. Rev. Mol. Cell Biol. 2:2001;569-577
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 569-577
    • Russell, D.G.1
  • 31
  • 33
    • 0037647196 scopus 로고    scopus 로고
    • An overview of the protein tyrosine phosphatase superfamily
    • Wang W.Q., Sun J.P., Zhang Z.Y. An overview of the protein tyrosine phosphatase superfamily. Curr. Top. Med. Chem. 3:2003;739-748
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 739-748
    • Wang, W.Q.1    Sun, J.P.2    Zhang, Z.Y.3
  • 34
    • 0037337317 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases
    • Young T.A., Delagoutte B., Endrizzi J.A., Falick A.M., Alber T. Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases. Nat. Struct. Biol. 10:2003;168-174
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 168-174
    • Young, T.A.1    Delagoutte, B.2    Endrizzi, J.A.3    Falick, A.M.4    Alber, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.