메뉴 건너뛰기




Volumn 191, Issue 15, 2009, Pages 4722-4731

The functional role of a conserved loop in EAL domain-based cyclic di-GMP-specific phosphodiesterase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYCLIC DI GMP PHOSPHODIESTERASE; CYCLIC GMP PHOSPHODIESTERASE; DEUTERIUM; DIGUANYLASE CYCLASE 2; GUANYLATE CYCLASE; HYDROGEN; MAGNESIUM ION; PROTEIN PA2567; PROTEIN ROCR; UNCLASSIFIED DRUG;

EID: 67749113278     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00327-09     Document Type: Article
Times cited : (93)

References (42)
  • 1
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • Arnold, K., L. Bordoli, J. Kopp, and T. Schwede. 2006. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 2
    • 84934438434 scopus 로고    scopus 로고
    • Regulation of biofilm formation in Yersinia pestis
    • Bobrov, A. G., V. Kirillina, and R. D. Perry. 2007. Regulation of biofilm formation in Yersinia pestis. Adv. Exp. Med. Biol. 603:201-210.
    • (2007) Adv. Exp. Med. Biol , vol.603 , pp. 201-210
    • Bobrov, A.G.1    Kirillina, V.2    Perry, R.D.3
  • 3
    • 0027440693 scopus 로고
    • Characterization of the functional role of a flexible loop in the alpha-subunit of tryptophan synthase from Salmonella typhimurium by rapid-scanning, stopped-flow spectroscopy and site-directed mutagenesis
    • Brzovic, P. S., C. C. Hyde, E. W. Miles, and M. F. Dunn. 1993. Characterization of the functional role of a flexible loop in the alpha-subunit of tryptophan synthase from Salmonella typhimurium by rapid-scanning, stopped-flow spectroscopy and site-directed mutagenesis. Biochemistry 32:10404-10413.
    • (1993) Biochemistry , vol.32 , pp. 10404-10413
    • Brzovic, P.S.1    Hyde, C.C.2    Miles, E.W.3    Dunn, M.F.4
  • 4
    • 0026715868 scopus 로고
    • Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex
    • Brzovic, P. S., Y. Sawa, C. C. Hyde, E. W. Miles, and M. F. Dunn. 1992. Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex. J. Biol. Chem. 267:13028-13038.
    • (1992) J. Biol. Chem , vol.267 , pp. 13028-13038
    • Brzovic, P.S.1    Sawa, Y.2    Hyde, C.C.3    Miles, E.W.4    Dunn, M.F.5
  • 5
    • 33644517930 scopus 로고    scopus 로고
    • Bacterial small-molecule signaling pathways
    • Camilli, A., and B. L. Bassler. 2006. Bacterial small-molecule signaling pathways. Science 311:1113-1116.
    • (2006) Science , vol.311 , pp. 1113-1116
    • Camilli, A.1    Bassler, B.L.2
  • 6
    • 2442555149 scopus 로고    scopus 로고
    • Crystal structure and amide H/D exchange of binary complexes of alcohol dehydrogenase from Bacillus stearothermophilus: Insight into thermostability and cofactor binding
    • Ceccarelli, C., Z. X. Liang, M. Strickler, G. Prehna, B. M. Goldstein, J. P. Klinman, and B. J. Bahnson. 2004. Crystal structure and amide H/D exchange of binary complexes of alcohol dehydrogenase from Bacillus stearothermophilus: insight into thermostability and cofactor binding. Biochemistry 43:5266-5277.
    • (2004) Biochemistry , vol.43 , pp. 5266-5277
    • Ceccarelli, C.1    Liang, Z.X.2    Strickler, M.3    Prehna, G.4    Goldstein, B.M.5    Klinman, J.P.6    Bahnson, B.J.7
  • 9
    • 24744457756 scopus 로고    scopus 로고
    • Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP
    • Christen, M., B. Christen, M. Folcher, A. Schauerte, and U. Jenal. 2005. Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP. J. Biol. Chem. 280:30829-30837.
    • (2005) J. Biol. Chem , vol.280 , pp. 30829-30837
    • Christen, M.1    Christen, B.2    Folcher, M.3    Schauerte, A.4    Jenal, U.5
  • 10
    • 4744349524 scopus 로고    scopus 로고
    • Role of the GGDEF protein family in Salmonella cellulose biosynthesis and biofilm formation
    • Garcia, B., C. Latasa, C. Solano, F. G. Portillo, C. Gamazo, and I. Lasa. 2004. Role of the GGDEF protein family in Salmonella cellulose biosynthesis and biofilm formation. Mol. Microbiol. 54:264-277.
    • (2004) Mol. Microbiol , vol.54 , pp. 264-277
    • Garcia, B.1    Latasa, C.2    Solano, C.3    Portillo, F.G.4    Gamazo, C.5    Lasa, I.6
  • 11
    • 34848889244 scopus 로고    scopus 로고
    • A comprehensive genetic characterization of bacterial motility
    • Girgis, H. S., Y. Liu, W. S. Ryu, and S. Tavazoie. 2007. A comprehensive genetic characterization of bacterial motility. PLOS Genet. 3:1644-1660.
    • (2007) PLOS Genet , vol.3 , pp. 1644-1660
    • Girgis, H.S.1    Liu, Y.2    Ryu, W.S.3    Tavazoie, S.4
  • 12
    • 38949203822 scopus 로고    scopus 로고
    • Interaction of CheY with the C-terminal peptide of CheZ
    • Guhaniyogi, J., T. Wu, S. S. Patel, and A. M. Stock. 2008. Interaction of CheY with the C-terminal peptide of CheZ. J. Bacteriol. 190:1419-1428.
    • (2008) J. Bacteriol , vol.190 , pp. 1419-1428
    • Guhaniyogi, J.1    Wu, T.2    Patel, S.S.3    Stock, A.M.4
  • 14
    • 33845403359 scopus 로고    scopus 로고
    • Mechanisms of cyclic-di-GMP signaling in bacteria
    • Jenal, U., and J. Malone. 2006. Mechanisms of cyclic-di-GMP signaling in bacteria. Annu. Rev. Genet. 40:385-407.
    • (2006) Annu. Rev. Genet , vol.40 , pp. 385-407
    • Jenal, U.1    Malone, J.2
  • 15
    • 0025015392 scopus 로고
    • Anatomy of a conformational change: Hinged "lid" motion of the triosephosphate isomerase loop
    • Joseph, D., G. A. Petsko, and M. Karplus. 1990. Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop. Science 249:1425-1428.
    • (1990) Science , vol.249 , pp. 1425-1428
    • Joseph, D.1    Petsko, G.A.2    Karplus, M.3
  • 16
    • 33646397872 scopus 로고    scopus 로고
    • Analysis of fimX, a phosphodiesterase that governs twitching motility in Pseudomonas aeruginosa
    • Kazmierczak, B. I., M. B. Lebron, and T. S. Murray. 2006. Analysis of fimX, a phosphodiesterase that governs twitching motility in Pseudomonas aeruginosa. Mol. Microbiol. 60:1026-1043.
    • (2006) Mol. Microbiol , vol.60 , pp. 1026-1043
    • Kazmierczak, B.I.1    Lebron, M.B.2    Murray, T.S.3
  • 17
    • 36549021125 scopus 로고    scopus 로고
    • BifA, a cyclic-di-GMP phosphodiesterase, inversely regulates biofilm formation and swarming motility by Pseudomonas aeruginosa PA14
    • Kuchma, S. L., K. M. Brothers, J. H. Merritt, N. T. Liberati, F. M. Ausubel, and G. A. O'Toole. 2007. BifA, a cyclic-di-GMP phosphodiesterase, inversely regulates biofilm formation and swarming motility by Pseudomonas aeruginosa PA14. J. Bacteriol. 189:8165-8178.
    • (2007) J. Bacteriol , vol.189 , pp. 8165-8178
    • Kuchma, S.L.1    Brothers, K.M.2    Merritt, J.H.3    Liberati, N.T.4    Ausubel, F.M.5    O'Toole, G.A.6
  • 18
    • 13144257722 scopus 로고    scopus 로고
    • A novel two-component system controls the expression of Pseudomonas aeruginosa fimbrial cup genes
    • Kulasekara, H. D., I. Ventre, B. R. Kulasekara, A. Lazdunski, A. Filloux, and S. Lory. 2005. A novel two-component system controls the expression of Pseudomonas aeruginosa fimbrial cup genes. Mol. Microbiol. 55:368-380.
    • (2005) Mol. Microbiol , vol.55 , pp. 368-380
    • Kulasekara, H.D.1    Ventre, I.2    Kulasekara, B.R.3    Lazdunski, A.4    Filloux, A.5    Lory, S.6
  • 19
    • 3042709505 scopus 로고    scopus 로고
    • Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase
    • Liang, Z. X., T. Lee, K. A. Resing, N. G. Ahn, and J. P. Klinman. 2004. Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase. Proc. Natl. Acad. Sci. USA 101:9556-9561.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9556-9561
    • Liang, Z.X.1    Lee, T.2    Resing, K.A.3    Ahn, N.G.4    Klinman, J.P.5
  • 20
    • 8744220635 scopus 로고    scopus 로고
    • Evidence for increased local flexibility in psychrophilic alcohol dehydrogenase relative to its thermophilic homologue
    • Liang, Z. X., I. Tsigos, T. Lee, V. Bouriotis, K. A. Resing, N. G. Ahn, and J. P. Klinman. 2004. Evidence for increased local flexibility in psychrophilic alcohol dehydrogenase relative to its thermophilic homologue. Biochemistry 43:14676-14683.
    • (2004) Biochemistry , vol.43 , pp. 14676-14683
    • Liang, Z.X.1    Tsigos, I.2    Lee, T.3    Bouriotis, V.4    Resing, K.A.5    Ahn, N.G.6    Klinman, J.P.7
  • 21
    • 0025741291 scopus 로고
    • Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate
    • Lundqvist, T., and G. Schneider. 1991. Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate. J. Biol. Chem. 266:12604-12611.
    • (1991) J. Biol. Chem , vol.266 , pp. 12604-12611
    • Lundqvist, T.1    Schneider, G.2
  • 22
    • 0034681940 scopus 로고    scopus 로고
    • Crystal structure at 2.4 A resolution of Borrelia burgdorferi inosine 5′-monophosphate dehydrogenase: Evidence of a substrate-induced hinged-lid motion by loop 6
    • McMillan, F. M., M. Cahoon, A. White, L. Hedstrom, G. A. Petsko, and D. Ringe. 2000. Crystal structure at 2.4 A resolution of Borrelia burgdorferi inosine 5′-monophosphate dehydrogenase: evidence of a substrate-induced hinged-lid motion by loop 6. Biochemistry 39:4533-4542.
    • (2000) Biochemistry , vol.39 , pp. 4533-4542
    • McMillan, F.M.1    Cahoon, M.2    White, A.3    Hedstrom, L.4    Petsko, G.A.5    Ringe, D.6
  • 24
    • 62549150834 scopus 로고    scopus 로고
    • Newell, P. D., R. D. Monds, and G. A. O'Toole. 13 February 2009. LapD is a bis-(3′,5′)-cyclic dimeric GMP-binding protein that regulates surface attachment by Pseudomonas fluorescens Pf0-1. Proc. Natl. Acad. Sci. USA doi:10.1073/pnas.0808933106.
    • Newell, P. D., R. D. Monds, and G. A. O'Toole. 13 February 2009. LapD is a bis-(3′,5′)-cyclic dimeric GMP-binding protein that regulates surface attachment by Pseudomonas fluorescens Pf0-1. Proc. Natl. Acad. Sci. USA doi:10.1073/pnas.0808933106.
  • 25
    • 0025276041 scopus 로고
    • Stabilization of a reaction intermediate as a catalytic device: Definition of the functional role of the flexible loop in triosephosphate isomerase
    • Pompliano, D. L., A. Peyman, and J. R. Knowles. 1990. Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase. Biochemistry 29:3186-3194.
    • (1990) Biochemistry , vol.29 , pp. 3186-3194
    • Pompliano, D.L.1    Peyman, A.2    Knowles, J.R.3
  • 26
  • 27
    • 67349108043 scopus 로고    scopus 로고
    • Enzymatic synthesis of c-di-GMP using a thermophilic diguanylate cyclase
    • Rao, F., S. Pasunooti, Y. Ng, W. Zhuo, L. Lim, W. Liu, and Z.-X. Liang. 2009. Enzymatic synthesis of c-di-GMP using a thermophilic diguanylate cyclase. Anal. Biochem. 389:138-142.
    • (2009) Anal. Biochem , vol.389 , pp. 138-142
    • Rao, F.1    Pasunooti, S.2    Ng, Y.3    Zhuo, W.4    Lim, L.5    Liu, W.6    Liang, Z.-X.7
  • 28
    • 47049115663 scopus 로고    scopus 로고
    • Catalytic mechanism of cyclic di-GMP-specific phosphodiesterase: A study of the EAL domain-containing RocR from Pseudomonas aeruginosa
    • Rao, F., Y. Yang, Y. Qi, and Z.-X. Liang. 2008. Catalytic mechanism of cyclic di-GMP-specific phosphodiesterase: a study of the EAL domain-containing RocR from Pseudomonas aeruginosa. J. Bacteriol. 190:3622-3631.
    • (2008) J. Bacteriol , vol.190 , pp. 3622-3631
    • Rao, F.1    Yang, Y.2    Qi, Y.3    Liang, Z.-X.4
  • 29
    • 0033474495 scopus 로고    scopus 로고
    • Modeling deuterium exchange behavior of ERK2 using pepsin mapping to probe secondary structure
    • Resing, K. A., A. N. Hoofnagle, and N. G. Ahn. 1999. Modeling deuterium exchange behavior of ERK2 using pepsin mapping to probe secondary structure. Am. Soc. Mass. Spectrom. 10:685-702.
    • (1999) Am. Soc. Mass. Spectrom , vol.10 , pp. 685-702
    • Resing, K.A.1    Hoofnagle, A.N.2    Ahn, N.G.3
  • 30
    • 22644438480 scopus 로고    scopus 로고
    • c-di-GMP: The dawning of a novel bacterial signalling system
    • Romling, U., M. Gomelsky, and M. Y. Galperin. 2005. c-di-GMP: the dawning of a novel bacterial signalling system. Mol. Microbiol. 57:629-639.
    • (2005) Mol. Microbiol , vol.57 , pp. 629-639
    • Romling, U.1    Gomelsky, M.2    Galperin, M.Y.3
  • 32
    • 21844451590 scopus 로고    scopus 로고
    • The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: Enzymatically active and inactive EAL domains
    • Schmidt, A. J., D. A. Ryjenkov, and M. Gomelsky. 2005. The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains. J. Bacteriol. 187:4774-4781.
    • (2005) J. Bacteriol , vol.187 , pp. 4774-4781
    • Schmidt, A.J.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 33
    • 34247566143 scopus 로고    scopus 로고
    • Role of EAL-containing proteins in multicellular behavior of Salmonella enterica serovar Typhimurium
    • Simm, R., A. Lusch, A. Kader, M. Andersson, and U. Romling. 2007. Role of EAL-containing proteins in multicellular behavior of Salmonella enterica serovar Typhimurium. J. Bacteriol. 189:3613-3623.
    • (2007) J. Bacteriol , vol.189 , pp. 3613-3623
    • Simm, R.1    Lusch, A.2    Kader, A.3    Andersson, M.4    Romling, U.5
  • 35
    • 0034739007 scopus 로고    scopus 로고
    • Stover, C. K., X. Q. Pham, A. L. Erwin, S. D. Mizoguchi, P. Warrener, M. J. Hickey, F. S. L. Brinkman, W. O. Hufnagle, D. J. Kowalik, M. Lagrou, R. L. Garber, L. Goltry, E. Tolentino, S. Westbrock-Wadman, Y. Yuan, L. L. Brody, S. N. Coulter, K. R. Folger, A. Kas, K. Larbig, R. Lim, K. Smith, D. Spencer, G. K. S. Wong, Z. Wu, I. T. Paulsen, J. Reizer, M. H. Saier, R. E. W. Hancock, S. Lory, and M. V. Olson. 2000. Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature 406:959-964.
    • Stover, C. K., X. Q. Pham, A. L. Erwin, S. D. Mizoguchi, P. Warrener, M. J. Hickey, F. S. L. Brinkman, W. O. Hufnagle, D. J. Kowalik, M. Lagrou, R. L. Garber, L. Goltry, E. Tolentino, S. Westbrock-Wadman, Y. Yuan, L. L. Brody, S. N. Coulter, K. R. Folger, A. Kas, K. Larbig, R. Lim, K. Smith, D. Spencer, G. K. S. Wong, Z. Wu, I. T. Paulsen, J. Reizer, M. H. Saier, R. E. W. Hancock, S. Lory, and M. V. Olson. 2000. Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature 406:959-964.
  • 36
    • 33748705968 scopus 로고    scopus 로고
    • Identification of a novel regulatory protein (CsrD) that targets the global regulatory RNAs CsrB and CsrC for degradation by RNase E
    • Suzuki, K., P. Babitzke, S. R. Kushner, and T. Romeo. 2006. Identification of a novel regulatory protein (CsrD) that targets the global regulatory RNAs CsrB and CsrC for degradation by RNase E. Genes Dev. 20:2605-2617.
    • (2006) Genes Dev , vol.20 , pp. 2605-2617
    • Suzuki, K.1    Babitzke, P.2    Kushner, S.R.3    Romeo, T.4
  • 38
    • 25144489145 scopus 로고    scopus 로고
    • The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase
    • Tamayo, R., A. D. Tischler, and A. Camilli. 2005. The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase. J. Biol. Chem. 280:33324-33330.
    • (2005) J. Biol. Chem , vol.280 , pp. 33324-33330
    • Tamayo, R.1    Tischler, A.D.2    Camilli, A.3
  • 39
    • 33845918217 scopus 로고    scopus 로고
    • An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turnover of the second messenger c-di-GMP
    • Tarutina, M., D. A. Ryjenkov, and M. Gomelsky. 2006. An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turnover of the second messenger c-di-GMP. J. Biol. Chem. 281:34751-34758.
    • (2006) J. Biol. Chem , vol.281 , pp. 34751-34758
    • Tarutina, M.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 40
    • 61449219844 scopus 로고    scopus 로고
    • The BLUF-EAL protein YcgF acts as a direct anti-repressor in a blue-light response of Escherichia coli
    • Tschowri, N., S. Busse, and R. Hengge. 2009. The BLUF-EAL protein YcgF acts as a direct anti-repressor in a blue-light response of Escherichia coli. Genes Dev. 23:522-534.
    • (2009) Genes Dev , vol.23 , pp. 522-534
    • Tschowri, N.1    Busse, S.2    Hengge, R.3
  • 41
    • 33750432511 scopus 로고    scopus 로고
    • Cyclic-di-GMP-mediated signalling within the sigma(S) network of Escherichia coli
    • Weber, H., C. Persavento, G. Possling, G. Tischendorf, and R. Hengge. 2006. Cyclic-di-GMP-mediated signalling within the sigma(S) network of Escherichia coli. Mol. Microbiol. 62:1014-1034.
    • (2006) Mol. Microbiol , vol.62 , pp. 1014-1034
    • Weber, H.1    Persavento, C.2    Possling, G.3    Tischendorf, G.4    Hengge, R.5
  • 42
    • 33751337111 scopus 로고    scopus 로고
    • Semi-automated analysis of hydrogen exchange mass spectra using HX-Express
    • Weis, D. D., I. J. Kass, and J. R. Engen. 2006. Semi-automated analysis of hydrogen exchange mass spectra using HX-Express. J. Am. Soc. Mass. Spectrom. 17:1700-1703.
    • (2006) J. Am. Soc. Mass. Spectrom , vol.17 , pp. 1700-1703
    • Weis, D.D.1    Kass, I.J.2    Engen, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.