메뉴 건너뛰기




Volumn 13, Issue 2, 2010, Pages 190-197

Interaction fidelity in two-component signaling

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOTRANSFERASE; PROTEIN HISTIDINE KINASE;

EID: 77949915674     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2010.01.007     Document Type: Review
Times cited : (51)

References (46)
  • 2
    • 36549003158 scopus 로고    scopus 로고
    • Sensor complexes regulating two-component signal transduction
    • Szurmant H., White R.A., and Hoch J.A. Sensor complexes regulating two-component signal transduction. Curr Opin Struct Biol 17 (2007) 706-715
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 706-715
    • Szurmant, H.1    White, R.A.2    Hoch, J.A.3
  • 3
    • 33744983969 scopus 로고    scopus 로고
    • Structural classification of bacterial response regulators: diversity of output domains and domain combinations
    • Galperin M.Y. Structural classification of bacterial response regulators: diversity of output domains and domain combinations. J Bacteriol 188 (2006) 4169-4182
    • (2006) J Bacteriol , vol.188 , pp. 4169-4182
    • Galperin, M.Y.1
  • 4
    • 0034662751 scopus 로고    scopus 로고
    • A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction
    • This manuscript presents the first high-resolution insight into the SK/RR interaction specificity in the form of the Spo0B/Spo0F co-crystal structure. Although Spo0B is a phosphotransfer protein in the sporulation phosphorelay rather than a SK, the structure demonstrates that it shares fold and function with the SK. As such, this manuscript proved to be the major milestone in the understanding of signaling fidelity by revealing the contact interface between SK and RR.
    • Zapf J., Sen U., Madhusudan, Hoch J.A., and Varughese K.I. A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction. Structure 8 (2000) 851-862. This manuscript presents the first high-resolution insight into the SK/RR interaction specificity in the form of the Spo0B/Spo0F co-crystal structure. Although Spo0B is a phosphotransfer protein in the sporulation phosphorelay rather than a SK, the structure demonstrates that it shares fold and function with the SK. As such, this manuscript proved to be the major milestone in the understanding of signaling fidelity by revealing the contact interface between SK and RR.
    • (2000) Structure , vol.8 , pp. 851-862
    • Zapf, J.1    Sen, U.2    Madhusudan3    Hoch, J.A.4    Varughese, K.I.5
  • 5
    • 0024562159 scopus 로고
    • Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
    • Stock A.M., Mottonen J.M., Stock J.B., and Schutt C.E. Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis. Nature 337 (1989) 745-749
    • (1989) Nature , vol.337 , pp. 745-749
    • Stock, A.M.1    Mottonen, J.M.2    Stock, J.B.3    Schutt, C.E.4
  • 7
    • 0030585421 scopus 로고    scopus 로고
    • Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis
    • Madhusudan, Zapf J., Whiteley J.M., Hoch J.A., Xuong N.H., and Varughese K.I. Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis. Structure 4 (1996) 679-690
    • (1996) Structure , vol.4 , pp. 679-690
    • Madhusudan1    Zapf, J.2    Whiteley, J.M.3    Hoch, J.A.4    Xuong, N.H.5    Varughese, K.I.6
  • 8
    • 38549144166 scopus 로고    scopus 로고
    • The genomes on line database (GOLD) in 2007: status of genomic and metagenomic projects and their associated metadata
    • Liolios K., Mavromatis K., Tavernarakis N., and Kyrpides N.C. The genomes on line database (GOLD) in 2007: status of genomic and metagenomic projects and their associated metadata. Nucleic Acids Res 36 (2008) D475-479
    • (2008) Nucleic Acids Res , vol.36
    • Liolios, K.1    Mavromatis, K.2    Tavernarakis, N.3    Kyrpides, N.C.4
  • 9
    • 75549092201 scopus 로고    scopus 로고
    • The MiST2 database: a comprehensive genomics resource on microbial signal transduction
    • Ulrich L.E., and Zhulin I.B. The MiST2 database: a comprehensive genomics resource on microbial signal transduction. Nucleic Acids Res 38 (2010) D401-D407
    • (2010) Nucleic Acids Res , vol.38
    • Ulrich, L.E.1    Zhulin, I.B.2
  • 10
    • 23944523895 scopus 로고    scopus 로고
    • A census of membrane-bound and intracellular signal transduction proteins in bacteria: bacterial IQ, extroverts and introverts
    • Galperin M.Y. A census of membrane-bound and intracellular signal transduction proteins in bacteria: bacterial IQ, extroverts and introverts. BMC Microbiol 5 (2005) 35
    • (2005) BMC Microbiol , vol.5 , pp. 35
    • Galperin, M.Y.1
  • 11
    • 41749088673 scopus 로고    scopus 로고
    • Bacitracin sensing in Bacillus subtilis
    • Rietkotter E., Hoyer D., and Mascher T. Bacitracin sensing in Bacillus subtilis. Mol Microbiol 68 (2008) 768-785
    • (2008) Mol Microbiol , vol.68 , pp. 768-785
    • Rietkotter, E.1    Hoyer, D.2    Mascher, T.3
  • 12
    • 33645050137 scopus 로고    scopus 로고
    • Interactions between the YycFG and PhoPR two-component systems in Bacillus subtilis: the PhoR kinase phosphorylates the non-cognate YycF response regulator upon phosphate limitation
    • Howell A., Dubrac S., Noone D., Varughese K.I., and Devine K. Interactions between the YycFG and PhoPR two-component systems in Bacillus subtilis: the PhoR kinase phosphorylates the non-cognate YycF response regulator upon phosphate limitation. Mol Microbiol 59 (2006) 1199-1215
    • (2006) Mol Microbiol , vol.59 , pp. 1199-1215
    • Howell, A.1    Dubrac, S.2    Noone, D.3    Varughese, K.I.4    Devine, K.5
  • 13
    • 44449112421 scopus 로고    scopus 로고
    • Specificity in two-component signal transduction pathways
    • Laub M.T., and Goulian M. Specificity in two-component signal transduction pathways. Annu Rev Genet 41 (2007) 121-145
    • (2007) Annu Rev Genet , vol.41 , pp. 121-145
    • Laub, M.T.1    Goulian, M.2
  • 14
    • 12544258487 scopus 로고    scopus 로고
    • Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli
    • Yamamoto K., Hirao K., Oshima T., Aiba H., Utsumi R., and Ishihama A. Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli. J Biol Chem 280 (2005) 1448-1456
    • (2005) J Biol Chem , vol.280 , pp. 1448-1456
    • Yamamoto, K.1    Hirao, K.2    Oshima, T.3    Aiba, H.4    Utsumi, R.5    Ishihama, A.6
  • 15
    • 26444481955 scopus 로고    scopus 로고
    • Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis
    • Skerker J.M., Prasol M.S., Perchuk B.S., Biondi E.G., and Laub M.T. Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis. PLoS Biol 3 (2005) e334
    • (2005) PLoS Biol , vol.3
    • Skerker, J.M.1    Prasol, M.S.2    Perchuk, B.S.3    Biondi, E.G.4    Laub, M.T.5
  • 16
    • 0030813090 scopus 로고    scopus 로고
    • Molecular recognition in signal transduction: the interaction surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis
    • Tzeng Y.L., and Hoch J.A. Molecular recognition in signal transduction: the interaction surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis. J Mol Biol 272 (1997) 200-212
    • (1997) J Mol Biol , vol.272 , pp. 200-212
    • Tzeng, Y.L.1    Hoch, J.A.2
  • 17
    • 29244433095 scopus 로고    scopus 로고
    • Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein
    • Marina A., Waldburger C.D., and Hendrickson W.A. Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein. EMBO J 24 (2005) 4247-4259
    • (2005) EMBO J , vol.24 , pp. 4247-4259
    • Marina, A.1    Waldburger, C.D.2    Hendrickson, W.A.3
  • 18
    • 0032184886 scopus 로고    scopus 로고
    • Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase
    • Varughese K.I., Madhusudan, Zhou X.Z., Whiteley J.M., and Hoch J.A. Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase. Mol Cell 2 (1998) 485-493
    • (1998) Mol Cell , vol.2 , pp. 485-493
    • Varughese, K.I.1    Madhusudan2    Zhou, X.Z.3    Whiteley, J.M.4    Hoch, J.A.5
  • 19
    • 0025964291 scopus 로고
    • Initiation of sporulation in Bacillus subtilis is controlled by a multicomponent phosphorelay
    • Burbulys D., Trach K.A., and Hoch J.A. Initiation of sporulation in Bacillus subtilis is controlled by a multicomponent phosphorelay. Cell 64 (1991) 545-552
    • (1991) Cell , vol.64 , pp. 545-552
    • Burbulys, D.1    Trach, K.A.2    Hoch, J.A.3
  • 20
    • 0034035586 scopus 로고    scopus 로고
    • Two-component and phosphorelay signal transduction
    • Hoch J.A. Two-component and phosphorelay signal transduction. Curr Opin Microbiol 3 (2000) 165-170
    • (2000) Curr Opin Microbiol , vol.3 , pp. 165-170
    • Hoch, J.A.1
  • 21
    • 70349541000 scopus 로고    scopus 로고
    • Biological insights from structures of two-component proteins
    • Gao R., and Stock A.M. Biological insights from structures of two-component proteins. Annu Rev Microbiol 63 (2009) 133-154
    • (2009) Annu Rev Microbiol , vol.63 , pp. 133-154
    • Gao, R.1    Stock, A.M.2
  • 22
    • 33745471490 scopus 로고    scopus 로고
    • The crystal structure of beryllofluoride Spo0F in complex with the phosphotransferase Spo0B represents a phosphotransfer pretransition state
    • Varughese K.I., Tsigelny I., and Zhao H. The crystal structure of beryllofluoride Spo0F in complex with the phosphotransferase Spo0B represents a phosphotransfer pretransition state. J Bacteriol 188 (2006) 4970-4977
    • (2006) J Bacteriol , vol.188 , pp. 4970-4977
    • Varughese, K.I.1    Tsigelny, I.2    Zhao, H.3
  • 23
    • 0034879819 scopus 로고    scopus 로고
    • Keeping signals straight in phosphorelay signal transduction
    • Hoch J.A., and Varughese K.I. Keeping signals straight in phosphorelay signal transduction. J Bacteriol 183 (2001) 4941-4949
    • (2001) J Bacteriol , vol.183 , pp. 4941-4949
    • Hoch, J.A.1    Varughese, K.I.2
  • 24
    • 70349795241 scopus 로고    scopus 로고
    • Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction
    • The first structure of the prototypical SK HK853 in complex with its RR RR468 is presented. The structure reveals significant similarity with the Spo0B/Spo0F complex and contributes to our understanding of interaction fidelity in TCS signaling by revealing a few additional contact pairings.
    • Casino P., Rubio V., and Marina A. Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction. Cell 139 (2009) 325-336. The first structure of the prototypical SK HK853 in complex with its RR RR468 is presented. The structure reveals significant similarity with the Spo0B/Spo0F complex and contributes to our understanding of interaction fidelity in TCS signaling by revealing a few additional contact pairings.
    • (2009) Cell , vol.139 , pp. 325-336
    • Casino, P.1    Rubio, V.2    Marina, A.3
  • 25
    • 70349764676 scopus 로고    scopus 로고
    • Structure of PAS-linked histidine kinase and the response regulator complex
    • Yamada S., Sugimoto H., Kobayashi M., Ohno A., Nakamura H., and Shiro Y. Structure of PAS-linked histidine kinase and the response regulator complex. Structure 17 (2009) 1333-1344
    • (2009) Structure , vol.17 , pp. 1333-1344
    • Yamada, S.1    Sugimoto, H.2    Kobayashi, M.3    Ohno, A.4    Nakamura, H.5    Shiro, Y.6
  • 26
    • 34447104524 scopus 로고    scopus 로고
    • Features of protein-protein interactions in two-component signaling deduced from genomic libraries
    • This study is the first to apply co-variance analysis between SK and RR proteins to gain insights into the SK/RR contact residue pairs and introduces a scoring function to predict SK/RR interaction partners. The residue pairings predicted to confer interaction specificity have been experimentally validated in other studies.
    • White R.A., Szurmant H., Hoch J.A., and Hwa T. Features of protein-protein interactions in two-component signaling deduced from genomic libraries. Methods Enzymol 422 (2007) 75-101. This study is the first to apply co-variance analysis between SK and RR proteins to gain insights into the SK/RR contact residue pairs and introduces a scoring function to predict SK/RR interaction partners. The residue pairings predicted to confer interaction specificity have been experimentally validated in other studies.
    • (2007) Methods Enzymol , vol.422 , pp. 75-101
    • White, R.A.1    Szurmant, H.2    Hoch, J.A.3    Hwa, T.4
  • 27
    • 39149114704 scopus 로고    scopus 로고
    • Accurate prediction of protein-protein interactions from sequence alignments using a Bayesian method
    • In this manuscript a Bayesian network approach aimed at identifying protein interaction partners is presented and applied to two-component systems. The approach is mathematically distinct from the co-variance analysis by White et al. Interestingly both methods extract largely the same specificity conferring residue positions.
    • Burger L., and van Nimwegen E. Accurate prediction of protein-protein interactions from sequence alignments using a Bayesian method. Mol Syst Biol 4 (2008) 165. In this manuscript a Bayesian network approach aimed at identifying protein interaction partners is presented and applied to two-component systems. The approach is mathematically distinct from the co-variance analysis by White et al. Interestingly both methods extract largely the same specificity conferring residue positions.
    • (2008) Mol Syst Biol , vol.4 , pp. 165
    • Burger, L.1    van Nimwegen, E.2
  • 28
    • 58549114185 scopus 로고    scopus 로고
    • Identification of direct residue contacts in protein-protein interaction by message passing
    • In this study the co-variance approach introduced by White et al. is amended by a statistical inference step, which disentangles direct and indirect contributions to the observed co-variation of residue pairings. The new method referred to as direct coupling analysis strongly improves the predictive power of co-variance in identifying interaction surface contact residues and might find broad applicability to study elusive protein complexes.
    • Weigt M., White R.A., Szurmant H., Hoch J.A., and Hwa T. Identification of direct residue contacts in protein-protein interaction by message passing. Proc Natl Acad Sci U S A 106 (2009) 67-72. In this study the co-variance approach introduced by White et al. is amended by a statistical inference step, which disentangles direct and indirect contributions to the observed co-variation of residue pairings. The new method referred to as direct coupling analysis strongly improves the predictive power of co-variance in identifying interaction surface contact residues and might find broad applicability to study elusive protein complexes.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 67-72
    • Weigt, M.1    White, R.A.2    Szurmant, H.3    Hoch, J.A.4    Hwa, T.5
  • 29
    • 0028295169 scopus 로고
    • Correlated mutations and residue contacts in proteins
    • Göbel U., Sander C., Schneider R., and Valencia A. Correlated mutations and residue contacts in proteins. Proteins 18 (1994) 309-317
    • (1994) Proteins , vol.18 , pp. 309-317
    • Göbel, U.1    Sander, C.2    Schneider, R.3    Valencia, A.4
  • 30
    • 0033977832 scopus 로고    scopus 로고
    • Correlations among amino acid sites in bHLH protein domains: an information theoretic analysis
    • Atchley W.R., Wollenberg K.R., Fitch W.M., Terhalle W., and Dress A.W. Correlations among amino acid sites in bHLH protein domains: an information theoretic analysis. Mol Biol Evol 17 (2000) 164-178
    • (2000) Mol Biol Evol , vol.17 , pp. 164-178
    • Atchley, W.R.1    Wollenberg, K.R.2    Fitch, W.M.3    Terhalle, W.4    Dress, A.W.5
  • 31
    • 0023660022 scopus 로고
    • Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacco mosaic virus
    • Altschuh D., Lesk A.M., Bloomer A.C., and Klug A. Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacco mosaic virus. J Mol Biol 193 (1987) 693-707
    • (1987) J Mol Biol , vol.193 , pp. 693-707
    • Altschuh, D.1    Lesk, A.M.2    Bloomer, A.C.3    Klug, A.4
  • 32
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless S.W., and Ranganathan R. Evolutionarily conserved pathways of energetic connectivity in protein families. Science 286 (1999) 295-299
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 33
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel G.M., Lockless S.W., Wall M.A., and Ranganathan R. Evolutionarily conserved networks of residues mediate allosteric communication in proteins. Nat Struct Biol 10 (2003) 59-69
    • (2003) Nat Struct Biol , vol.10 , pp. 59-69
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 34
    • 84856043672 scopus 로고
    • A mathematical theory of communication
    • Shannon C.E. A mathematical theory of communication. Bell Syst Tech J 27 (1948) 379-423
    • (1948) Bell Syst Tech J , vol.27 , pp. 379-423
    • Shannon, C.E.1
  • 35
    • 0037447059 scopus 로고    scopus 로고
    • Amino acids determining enzyme-substrate specificity in prokaryotic and eukaryotic protein kinases
    • Li L., Shakhnovich E.I., and Mirny L.A. Amino acids determining enzyme-substrate specificity in prokaryotic and eukaryotic protein kinases. Proc Natl Acad Sci U S A 100 (2003) 4463-4468
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 4463-4468
    • Li, L.1    Shakhnovich, E.I.2    Mirny, L.A.3
  • 36
    • 44649153450 scopus 로고    scopus 로고
    • Rewiring the specificity of two-component signal transduction systems
    • A co-variance approach analogous to the earlier one by White et al. is presented. The authors utilize this information to rewire several SK proteins by site-directed mutagenesis to phosphorylate non-native RR targets.
    • Skerker J.M., Perchuk B.S., Siryaporn A., Lubin E.A., Ashenberg O., Goulian M., and Laub M.T. Rewiring the specificity of two-component signal transduction systems. Cell 133 (2008) 1043-1054. A co-variance approach analogous to the earlier one by White et al. is presented. The authors utilize this information to rewire several SK proteins by site-directed mutagenesis to phosphorylate non-native RR targets.
    • (2008) Cell , vol.133 , pp. 1043-1054
    • Skerker, J.M.1    Perchuk, B.S.2    Siryaporn, A.3    Lubin, E.A.4    Ashenberg, O.5    Goulian, M.6    Laub, M.T.7
  • 37
    • 38849115223 scopus 로고    scopus 로고
    • Mutual information without the influence of phylogeny or entropy dramatically improves residue contact prediction
    • Dunn S.D., Wahl L.M., and Gloor G.B. Mutual information without the influence of phylogeny or entropy dramatically improves residue contact prediction. Bioinformatics 24 (2008) 333-340
    • (2008) Bioinformatics , vol.24 , pp. 333-340
    • Dunn, S.D.1    Wahl, L.M.2    Gloor, G.B.3
  • 38
    • 0029988249 scopus 로고    scopus 로고
    • Altered recognition mutants of the response regulator PhoB: a new genetic strategy for studying protein-protein interactions
    • Haldimann A., Prahalad M.K., Fisher S.L., Kim S.K., Walsh C.T., and Wanner B.L. Altered recognition mutants of the response regulator PhoB: a new genetic strategy for studying protein-protein interactions. Proc Natl Acad Sci U S A 93 (1996) 14361-14366
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 14361-14366
    • Haldimann, A.1    Prahalad, M.K.2    Fisher, S.L.3    Kim, S.K.4    Walsh, C.T.5    Wanner, B.L.6
  • 39
    • 0032993415 scopus 로고    scopus 로고
    • Alanine mutants of the Spo0F response regulator modifying specificity for sensor kinases in sporulation initiation
    • Jiang M., Tzeng Y.L., Feher V.A., Perego M., and Hoch J.A. Alanine mutants of the Spo0F response regulator modifying specificity for sensor kinases in sporulation initiation. Mol Microbiol 33 (1999) 389-395
    • (1999) Mol Microbiol , vol.33 , pp. 389-395
    • Jiang, M.1    Tzeng, Y.L.2    Feher, V.A.3    Perego, M.4    Hoch, J.A.5
  • 40
    • 48249148736 scopus 로고    scopus 로고
    • Co-evolving motions at protein-protein interfaces of two-component signaling systems identified by covariance analysis
    • Szurmant H., Bobay B.G., White R.A., Sullivan D.M., Thompson R.J., Hwa T., Hoch J.A., and Cavanagh J. Co-evolving motions at protein-protein interfaces of two-component signaling systems identified by covariance analysis. Biochemistry 47 (2008) 7782-7784
    • (2008) Biochemistry , vol.47 , pp. 7782-7784
    • Szurmant, H.1    Bobay, B.G.2    White, R.A.3    Sullivan, D.M.4    Thompson, R.J.5    Hwa, T.6    Hoch, J.A.7    Cavanagh, J.8
  • 42
    • 76049105937 scopus 로고    scopus 로고
    • High resolution protein complexes from integrating genomic information with molecular simulation
    • This study presents a molecular dynamics approach to assemble high-resolution structures of protein complexes that utilizes individual proteins structures and protein-protein contacts derived from the DCA approach by Weigt et al.
    • Schug A., Weigt M., Onuchic J.N., Hwa T., and Szurmant H. High resolution protein complexes from integrating genomic information with molecular simulation. Proc Natl Acad Sci U S A 106 (2009) 22124-22129. This study presents a molecular dynamics approach to assemble high-resolution structures of protein complexes that utilizes individual proteins structures and protein-protein contacts derived from the DCA approach by Weigt et al.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 22124-22129
    • Schug, A.1    Weigt, M.2    Onuchic, J.N.3    Hwa, T.4    Szurmant, H.5
  • 43
    • 77949913363 scopus 로고    scopus 로고
    • Computational modeling of phosphotransfer complexes in two-component signaling
    • Schug A., Weigt M., Hoch J.A., Onuchic J.N., Hwa T., and Szurmant H. Computational modeling of phosphotransfer complexes in two-component signaling. Methods Enzymol 471 (2010) 43-58
    • (2010) Methods Enzymol , vol.471 , pp. 43-58
    • Schug, A.1    Weigt, M.2    Hoch, J.A.3    Onuchic, J.N.4    Hwa, T.5    Szurmant, H.6
  • 45
    • 37449018128 scopus 로고    scopus 로고
    • Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of SLN1 bound to a phosphoryl analog
    • Zhao X., Copeland D.M., Soares A.S., and West A.H. Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of SLN1 bound to a phosphoryl analog. J Mol Biol 375 (2008) 1141-1151
    • (2008) J Mol Biol , vol.375 , pp. 1141-1151
    • Zhao, X.1    Copeland, D.M.2    Soares, A.S.3    West, A.H.4
  • 46
    • 0344436666 scopus 로고    scopus 로고
    • The yeast YPD1/SLN1 complex: insights into molecular recognition in two-component signaling systems
    • Here the first high-resolution complex between a phosphorelay Hpt-type phosphotransferase and a RR is presented. The structure serves as the only representative model of the Hpt/RR complex, which is distinct from the HisKA-type SK/RR complex.
    • Xu Q., Porter S.W., and West A.H. The yeast YPD1/SLN1 complex: insights into molecular recognition in two-component signaling systems. Structure 11 (2003) 1569-1581. Here the first high-resolution complex between a phosphorelay Hpt-type phosphotransferase and a RR is presented. The structure serves as the only representative model of the Hpt/RR complex, which is distinct from the HisKA-type SK/RR complex.
    • (2003) Structure , vol.11 , pp. 1569-1581
    • Xu, Q.1    Porter, S.W.2    West, A.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.