메뉴 건너뛰기




Volumn 58, Issue 2, 2005, Pages 358-366

Structure and mechanism of Escherichia coli RecA ATPase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; RECA PROTEIN;

EID: 26944459614     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2005.04876.x     Document Type: Review
Times cited : (84)

References (58)
  • 1
    • 0030664070 scopus 로고    scopus 로고
    • An interaction between a specified surface of the C-terminal domain of RecA protein and double-stranded DNA for homologous pairing
    • Aihara, H., Ito, Y., Kurumizaka, H., Terada, T., Yokoyama, S., and Shibata, T. (1997) An interaction between a specified surface of the C-terminal domain of RecA protein and double-stranded DNA for homologous pairing. J Mol Biol 274:213-221.
    • (1997) J Mol Biol , vol.274 , pp. 213-221
    • Aihara, H.1    Ito, Y.2    Kurumizaka, H.3    Terada, T.4    Yokoyama, S.5    Shibata, T.6
  • 2
    • 0033538424 scopus 로고    scopus 로고
    • The N-terminal domain of the human Rad51 protein binds DNA: Structure and a DNA binding surface as revealed by NMR
    • Aihara, H., Ito, Y., Kurumizaka, H., Yokoyama, S., and Shibata, T. (1999) The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR. J Mol Biol 290: 495-504.
    • (1999) J Mol Biol , vol.290 , pp. 495-504
    • Aihara, H.1    Ito, Y.2    Kurumizaka, H.3    Yokoyama, S.4    Shibata, T.5
  • 3
    • 14844355639 scopus 로고    scopus 로고
    • Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA
    • Ariza, A., Richard, D.U., White, M.F., and Bond, C.S. (2005) Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA. Nucleic Acids Res 33: 1465-1473.
    • (2005) Nucleic Acids Res , vol.33 , pp. 1465-1473
    • Ariza, A.1    Richard, D.U.2    White, M.F.3    Bond, C.S.4
  • 4
    • 0023685553 scopus 로고    scopus 로고
    • Increase of DNA strand assimilation activity of recA protein by removal of the C terminus and structure-function studies of the resulting protein fragment
    • Benedict, R.C., and Kowalczykowski, S.C. (1998) Increase of DNA strand assimilation activity of recA protein by removal of the C terminus and structure-function studies of the resulting protein fragment. J Biol Chem 263: 15513-15520.
    • (1998) J Biol Chem , vol.263 , pp. 15513-15520
    • Benedict, R.C.1    Kowalczykowski, S.C.2
  • 5
    • 0001865832 scopus 로고    scopus 로고
    • DNA strand exchange proteins: A biochemical and physical comparison
    • Bianco, P.R., Tracy, R.B., and Kowalczykowski, S.C. (1998) DNA strand exchange proteins: a biochemical and physical comparison. Frontiers Biosci 3: 570-603.
    • (1998) Frontiers Biosci , vol.3 , pp. 570-603
    • Bianco, P.R.1    Tracy, R.B.2    Kowalczykowski, S.C.3
  • 6
    • 0033582802 scopus 로고    scopus 로고
    • On the in vivo function of the RecA ATPase
    • Campbell, M.J., and Davis, R.W. (1999) On the in vivo function of the RecA ATPase. J Mol Biol 286: 437-445.
    • (1999) J Mol Biol , vol.286 , pp. 437-445
    • Campbell, M.J.1    Davis, R.W.2
  • 8
    • 0242692609 scopus 로고    scopus 로고
    • The bacterial RecA protein as a motor protein
    • Cox, M.M. (2003) The bacterial RecA protein as a motor protein. Annu Rev Microbiol 57: 551-577.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 551-577
    • Cox, M.M.1
  • 10
    • 15744376313 scopus 로고    scopus 로고
    • Organized unidirectional waves of ATP hydrolysis within a RecA filament
    • Cox, J.M., Tsodikov, O.V., and Cox, M.M. (2005) Organized unidirectional waves of ATP hydrolysis within a RecA filament. PLOS Biol 3: 231-243.
    • (2005) PLOS Biol , vol.3 , pp. 231-243
    • Cox, J.M.1    Tsodikov, O.V.2    Cox, M.M.3
  • 12
    • 0037441480 scopus 로고    scopus 로고
    • Structural studies on MtRecA-nucleotide complexes: Insights into DNA and nucleotide binding and the structural signature of NTP recognition
    • Datta, S., Ganesh, N., Chandra, N.R., Muniappa, K., and Vijayan, M. (2003a) Structural studies on MtRecA-nucleotide complexes: insights into DNA and nucleotide binding and the structural signature of NTP recognition. Prot Struct Funct Gen 50: 474-485.
    • (2003) Prot Struct Funct Gen , vol.50 , pp. 474-485
    • Datta, S.1    Ganesh, N.2    Chandra, N.R.3    Muniappa, K.4    Vijayan, M.5
  • 13
    • 0038153902 scopus 로고    scopus 로고
    • Crystal structures of Mycobacterium smegmatis RecA and its nucleotide complexes
    • Datta, S., Krishna, R., Ganesh, N., Chandra, N.R., Muniyappa, K., and Vijayan, M. (2003b) Crystal structures of Mycobacterium smegmatis RecA and its nucleotide complexes. J Bacteriol 185: 4280-4284.
    • (2003) J Bacteriol , vol.185 , pp. 4280-4284
    • Datta, S.1    Krishna, R.2    Ganesh, N.3    Chandra, N.R.4    Muniyappa, K.5    Vijayan, M.6
  • 14
    • 0020475459 scopus 로고
    • Characterization of complexes between RecA protein and duplex DNA by electron microscopy
    • DiCapua, E., Engel, A., Stasiak, A., and Koller, T. (1982) Characterization of complexes between RecA protein and duplex DNA by electron microscopy. J Mol Biol 157: 87-104.
    • (1982) J Mol Biol , vol.157 , pp. 87-104
    • Dicapua, E.1    Engel, A.2    Stasiak, A.3    Koller, T.4
  • 15
    • 0000800256 scopus 로고
    • Electron microscopy of RecA-DNA complexes: Two different states, their functional significance and relation to the solved crystal structure
    • Egelman, E.H., and Stasiak, A. (1993) Electron microscopy of RecA-DNA complexes: two different states, their functional significance and relation to the solved crystal structure. Micron 24: 309-324.
    • (1993) Micron , vol.24 , pp. 309-324
    • Egelman, E.H.1    Stasiak, A.2
  • 16
    • 0038276074 scopus 로고    scopus 로고
    • The C terminus of the Escherichia coli RecA protein modulates the DNA binding competition with single-stranded DNA-binding protein
    • Eggler, A.L., Lusetti, S.L., and Cox, M.M. (2003) The C terminus of the Escherichia coli RecA protein modulates the DNA binding competition with single-stranded DNA-binding protein. J Biol Chem 278: 16389-16396.
    • (2003) J Biol Chem , vol.278 , pp. 16389-16396
    • Eggler, A.L.1    Lusetti, S.L.2    Cox, M.M.3
  • 17
    • 0028131478 scopus 로고
    • On the role of ATP hydrolysis in RecA protein-mediated DNA strand-exchange III. Unidirectional branch migration and extensive hybrid DNA formation
    • Jain, S.K., Cox, M.M., and Inman, R.B. (1994) On the role of ATP hydrolysis in RecA protein-mediated DNA strand-exchange III. Unidirectional branch migration and extensive hybrid DNA formation. J Biol Chem 269: 20653-20661.
    • (1994) J Biol Chem , vol.269 , pp. 20653-20661
    • Jain, S.K.1    Cox, M.M.2    Inman, R.B.3
  • 19
    • 0026737631 scopus 로고
    • On the role of ATP hydrolysis in RecA protein-mediated DNA strand exchange I. Bypassing a short heterologous insert in one DNA substrate
    • Kim, J.I., Cox, M.M., and Inman, R.B. (1992a) On the role of ATP hydrolysis in RecA protein-mediated DNA strand exchange I. Bypassing a short heterologous insert in one DNA substrate. J Biol Chem 267: 16438-16443.
    • (1992) J Biol Chem , vol.267 , pp. 16438-16443
    • Kim, J.I.1    Cox, M.M.2    Inman, R.B.3
  • 20
    • 0026662981 scopus 로고
    • On the role of ATP hydrolysis in RecA protein-mediated DNA strand exchange II. Four-strand exchanges
    • Kim, J.I., Cox, M.M., and Inman, R.B. (1992b) On the role of ATP hydrolysis in RecA protein-mediated DNA strand exchange II. Four-strand exchanges. J Biol Chem 267: 16444-16449.
    • (1992) J Biol Chem , vol.267 , pp. 16444-16449
    • Kim, J.I.1    Cox, M.M.2    Inman, R.B.3
  • 21
    • 2342466755 scopus 로고    scopus 로고
    • Structural basis for octameric ring formation and DNA interaction of the human homologous-pairing protein Dmc1
    • Kinebuchi, T., Kagawa, W., Enomoto, R., Tanaka, K., Miyagawa, K., Shibata, T., et al. (2004) Structural basis for octameric ring formation and DNA interaction of the human homologous-pairing protein Dmc1. Mol Cell 14: 363-374.
    • (2004) Mol Cell , vol.14 , pp. 363-374
    • Kinebuchi, T.1    Kagawa, W.2    Enomoto, R.3    Tanaka, K.4    Miyagawa, K.5    Shibata, T.6
  • 22
    • 0028297545 scopus 로고
    • Functional characterization of residues in the P-loop motif of the RecA protein ATP binding site
    • Konola, J.T., Logan, K.M., and Knight, K.L. (1994) Functional characterization of residues in the P-loop motif of the RecA protein ATP binding site. J Mol Biol 237: 20-34.
    • (1994) J Mol Biol , vol.237 , pp. 20-34
    • Konola, J.T.1    Logan, K.M.2    Knight, K.L.3
  • 23
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24: 946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 24
    • 0030475011 scopus 로고    scopus 로고
    • A possible role of the C-terminal domain of the RecA protein: A gateway model for double-stranded DNA binding
    • Kurumizaka, H., Auhara, H., Ikawa, S., Kashima, T., Bazemore, L.R., Kawasaki, K., et al. (1996) A possible role of the C-terminal domain of the RecA protein: a gateway model for double-stranded DNA binding. J Biol Chem 71: 33515-33524.
    • (1996) J Biol Chem , vol.71 , pp. 33515-33524
    • Kurumizaka, H.1    Auhara, H.2    Ikawa, S.3    Kashima, T.4    Bazemore, L.R.5    Kawasaki, K.6
  • 25
    • 0343188817 scopus 로고
    • Autodigestion of LexA and phage lambda repressors
    • Little, J.W. (1984) Autodigestion of LexA and phage lambda repressors. Proc Natl Acad Sci USA 81: 1375-1379.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 1375-1379
    • Little, J.W.1
  • 26
    • 0037938848 scopus 로고    scopus 로고
    • C-terminal deletions of the Escherichia coli RecA protein: Characterization of in vivo and in vitro effects
    • Lusetti, S.L., Wood, E.A., Fleming, C.D., Modica, M.J., Korth, J., Abbott, L., et al. (2003a) C-terminal deletions of the Escherichia coli RecA protein: characterization of in vivo and in vitro effects. J Biol Chem 278: 16372-16380.
    • (2003) J Biol Chem , vol.278 , pp. 16372-16380
    • Lusetti, S.L.1    Wood, E.A.2    Fleming, C.D.3    Modica, M.J.4    Korth, J.5    Abbott, L.6
  • 27
    • 0038276075 scopus 로고    scopus 로고
    • Magnesium ion-dependent activation of the RecA protein involves the C terminus
    • Lusetti, S.L., Shaw, J.J., and Cox, M.M. (2003b) Magnesium ion-dependent activation of the RecA protein involves the C terminus. J Biol Chem 278: 16381-16388.
    • (2003) J Biol Chem , vol.278 , pp. 16381-16388
    • Lusetti, S.L.1    Shaw, J.J.2    Cox, M.M.3
  • 28
    • 1642463787 scopus 로고    scopus 로고
    • Molecular design and functional organization of the RecA protein
    • McGrew, D.A., and Knight, K.L. (2003) Molecular design and functional organization of the RecA protein. Crit Rev Biochem Mol Biol 38: 385-432.
    • (2003) Crit Rev Biochem Mol Biol , vol.38 , pp. 385-432
    • McGrew, D.A.1    Knight, K.L.2
  • 30
    • 0029620927 scopus 로고
    • Photo cross-links between single-stranded DNA and Escherichia coli RecA protein map to loops L1 (amino acid residues 157-164) and L2 (amino acid residues 195-209)
    • Malkov, V.A., and Camerini-Otero, R.D. (1995) Photo cross-links between single-stranded DNA and Escherichia coli RecA protein map to loops L1 (amino acid residues 157-164) and L2 (amino acid residues 195-209). J Biol Chem 270:30230-30233.
    • (1995) J Biol Chem , vol.270 , pp. 30230-30233
    • Malkov, V.A.1    Camerini-Otero, R.D.2
  • 31
    • 0022429092 scopus 로고
    • Interaction of recA protein with single-stranded DNA. Quantitative aspects of binding affinity modulation by nucleotide cofactors
    • Menetski, J.P., and Kowalczykowski, S.C. (1985) Interaction of recA protein with single-stranded DNA. Quantitative aspects of binding affinity modulation by nucleotide cofactors. J Mol Biol 181: 281-295.
    • (1985) J Mol Biol , vol.181 , pp. 281-295
    • Menetski, J.P.1    Kowalczykowski, S.C.2
  • 32
    • 0025166577 scopus 로고
    • Stable DNA heteroduplex formation catalyzed by the Escherichia coli RecA protein in the absence of ATP hydrolysis
    • Menetski, J.P., Bear, D.G., and Kowalczykowski, S.C. (1990) Stable DNA heteroduplex formation catalyzed by the Escherichia coli RecA protein in the absence of ATP hydrolysis. Proc Natl Acad Sci USA 87: 21-25.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 21-25
    • Menetski, J.P.1    Bear, D.G.2    Kowalczykowski, S.C.3
  • 33
    • 0035838982 scopus 로고    scopus 로고
    • Structure of bovine mitrochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: Implications for the mechanism of rotary catalysis
    • Menz, R.I., Walker, J.E., and Leslie, A.G. (2001) Structure of bovine mitrochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis. Cell 106: 331-341.
    • (2001) Cell , vol.106 , pp. 331-341
    • Menz, R.I.1    Walker, J.E.2    Leslie, A.G.3
  • 34
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E.A., and Bacon, D.J. (1997) Raster3D: photorealistic molecular graphics. Methods Enzymol 277: 505-524.
    • (1997) Methods Enzymol , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 35
    • 2242443513 scopus 로고    scopus 로고
    • Insights into DNA recombination form the structure of a RAD51-BRCA2 complex
    • Pellegrini, L, Yu, D.S., Lo, T., Anand, S., Lee, M., Blundell, T.L., et al. (2002) Insights into DNA recombination form the structure of a RAD51-BRCA2 complex. Nature 420: 287-293.
    • (2002) Nature , vol.420 , pp. 287-293
    • Pellegrini, L.1    Yu, D.S.2    Lo, T.3    Anand, S.4    Lee, M.5    Blundell, T.L.6
  • 36
    • 8544258063 scopus 로고    scopus 로고
    • Crystal structure of RecA from Deinococcus radiodurans: Insights into the structural basis of extreme radioresistance
    • Rajan, R., and Bell, C.E. (2004) Crystal structure of RecA from Deinococcus radiodurans: insights into the structural basis of extreme radioresistance. J Mol Biol 344: 951-963.
    • (2004) J Mol Biol , vol.344 , pp. 951-963
    • Rajan, R.1    Bell, C.E.2
  • 37
    • 0027397313 scopus 로고
    • Alteration of the nucleoside triphosphate (NTP) catalytic domain within Escherichi coli recA protein attenuated NTP hydrolysis but not joint molecule formation
    • Rehrauer, W.M., and Kowalczykowski, S.C. (1993) Alteration of the nucleoside triphosphate (NTP) catalytic domain within Escherichi coli recA protein attenuated NTP hydrolysis but not joint molecule formation. J Biol Chem 268: 1292-1297.
    • (1993) J Biol Chem , vol.268 , pp. 1292-1297
    • Rehrauer, W.M.1    Kowalczykowski, S.C.2
  • 38
    • 0035902453 scopus 로고    scopus 로고
    • RecA protein promotes the regression of stalled replication forks in vitro
    • Robu, M.E., Inman, R.B., and Cox, M.M. (2001) RecA protein promotes the regression of stalled replication forks in vitro. Proc Natl Acad Sci USA 98: 8211-8218.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8211-8218
    • Robu, M.E.1    Inman, R.B.2    Cox, M.M.3
  • 40
    • 3142682325 scopus 로고    scopus 로고
    • XRCC2 enhances ADP/ATP processing and strand exchange by hRAD51
    • Shim, K.S., Schmutte, C., Tombline, G., Meinen, C.D., and Fishel, R. (2004) hXRCC2 enhances ADP/ATP processing and strand exchange by hRAD51. J Biol Chem 279: 30385-30394.
    • (2004) J Biol Chem , vol.279 , pp. 30385-30394
    • Shim, K.S.1    Schmutte, C.2    Tombline, G.3    Meinen, C.D.4    Fishel, R.5
  • 41
    • 0042738069 scopus 로고    scopus 로고
    • Full-length archaeal Rad51 structure and mutants: Mechanisms for RAD51 assembly and control by BRCA2
    • Shin, D.S., Pellegrini, L., Daniels, D.S., Yelent, B., Craig, L., Bates, D., et al. (2003) Full-length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2. EMBO J 22: 4566-4576.
    • (2003) EMBO J , vol.22 , pp. 4566-4576
    • Shin, D.S.1    Pellegrini, L.2    Daniels, D.S.3    Yelent, B.4    Craig, L.5    Bates, D.6
  • 42
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton, M.R., Sawaya, M.R., Ellenberger, T., and Wigley, D.B. (2000) Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 101: 589-600.
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 43
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story, R.M., and Steitz, T.A. (1992) Structure of the recA protein-ADP complex. Nature 355: 374-376.
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 44
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • Story, R.M., Weber, I.T., and Steitz, T.A. (1992) The structure of the E. coli recA protein monomer and polymer. Nature 355: 318-325.
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 45
    • 0026527367 scopus 로고
    • C-terminal truncated Escherichia coli RecA protein RecA5327 has enhanced binding affinities to single- And double-stranded DNAs
    • Tateishi, S., Horii, T., Ogawa, T., and Ogawa, H. (1992) C-terminal truncated Escherichia coli RecA protein RecA5327 has enhanced binding affinities to single- and double-stranded DNAs. J Mol Biol 223: 115-129.
    • (1992) J Mol Biol , vol.223 , pp. 115-129
    • Tateishi, S.1    Horii, T.2    Ogawa, T.3    Ogawa, H.4
  • 46
    • 0345276497 scopus 로고    scopus 로고
    • The crystal structure of the bifunctional primase-helicase of bacteriophage T7
    • Toth, E.A., Li, Y., Sawaya, M.R., Cheng, Y., and Ellenberger, T. (2003) The crystal structure of the bifunctional primase-helicase of bacteriophage T7. Mol Cell 12: 1113-1123.
    • (2003) Mol Cell , vol.12 , pp. 1113-1123
    • Toth, E.A.1    Li, Y.2    Sawaya, M.R.3    Cheng, Y.4    Ellenberger, T.5
  • 48
    • 0141757508 scopus 로고    scopus 로고
    • Complexes of RecA with LexA and RecX differentiate between active and inactive RecA nucleoprotein filaments
    • VanLoock, M.S., Yu, X., Yang, S., Galkin, V.E., Huang, H., Rajan, S.S., et al. (2003b) Complexes of RecA with LexA and RecX differentiate between active and inactive RecA nucleoprotein filaments. J Mol Biol 333: 345-354.
    • (2003) J Mol Biol , vol.333 , pp. 345-354
    • Vanloock, M.S.1    Yu, X.2    Yang, S.3    Galkin, V.E.4    Huang, H.5    Rajan, S.S.6
  • 49
    • 0029974806 scopus 로고    scopus 로고
    • Homologous DNA pairing promoted by a 20 amino acid peptide from RecA
    • Voloshin, O.N., Wang, L., and Camerini-Otero, R.D. (1996) Homologous DNA pairing promoted by a 20 amino acid peptide from RecA. Science 272: 868-872.
    • (1996) Science , vol.272 , pp. 868-872
    • Voloshin, O.N.1    Wang, L.2    Camerini-Otero, R.D.3
  • 50
    • 0034634390 scopus 로고    scopus 로고
    • The homologous pairing domain of RecA also mediates the allosteric regulation of DNA binding and ATP hydrolysis: A remarkable concentration of functional residues
    • Voloshin, O.N., Wang, L., and Camerini-Otero, R.D. (2000) The homologous pairing domain of RecA also mediates the allosteric regulation of DNA binding and ATP hydrolysis: a remarkable concentration of functional residues. J Mol Biol 303: 709-720.
    • (2000) J Mol Biol , vol.303 , pp. 709-720
    • Voloshin, O.N.1    Wang, L.2    Camerini-Otero, R.D.3
  • 51
    • 4143068081 scopus 로고    scopus 로고
    • Crystal structure of archaeal recombinase RadA: A snapshot of its extended conformation
    • Wu, Y., He, Y., Moya, I.A., Qian, X., and Luo, Y. (2004) Crystal structure of archaeal recombinase RadA: a snapshot of its extended conformation. Mol Cell 15: 423-435.
    • (2004) Mol Cell , vol.15 , pp. 423-435
    • Wu, Y.1    He, Y.2    Moya, I.A.3    Qian, X.4    Luo, Y.5
  • 52
    • 12844272179 scopus 로고    scopus 로고
    • Crystal structure of an ATPase-active form of Rad51 homolog from Methanococcus voltae: Insights into potassium dependence
    • Wu, Y., Qian, X., He, Y., Moya, I.A., and Luo, Y. (2005) Crystal structure of an ATPase-active form of Rad51 homolog from Methanococcus voltae: insights into potassium dependence. J Biol Chem 280: 722-728.
    • (2005) J Biol Chem , vol.280 , pp. 722-728
    • Wu, Y.1    Qian, X.2    He, Y.3    Moya, I.A.4    Luo, Y.5
  • 53
    • 4444308700 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli RecA in a compressed helical filament
    • Xing, X., and Bell, C.E. (2004a) Crystal structures of Escherichia coli RecA in a compressed helical filament. J Mol Biol 342: 1471-1485.
    • (2004) J Mol Biol , vol.342 , pp. 1471-1485
    • Xing, X.1    Bell, C.E.2
  • 54
    • 11144255128 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli RecA in complex with MgADP and MnAMP-PNP
    • Xing, X., and Bell, C.E. (2004b) Crystal structures of Escherichia coli RecA in complex with MgADP and MnAMP-PNP. Biochemistry 43: 16142-16152.
    • (2004) Biochemistry , vol.43 , pp. 16142-16152
    • Xing, X.1    Bell, C.E.2
  • 56
    • 0025783415 scopus 로고
    • Removal of RecA C-terminus results in a conformational change in the RecA-DNA filament
    • Yu, X., and Egelman, E.H. (1991) Removal of RecA C-terminus results in a conformational change in the RecA-DNA filament. J Struct Biol 106: 243-254.
    • (1991) J Struct Biol , vol.106 , pp. 243-254
    • Yu, X.1    Egelman, E.H.2
  • 57
    • 0035902614 scopus 로고    scopus 로고
    • Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA
    • Yu, X., Jacobs, S.A., West, S.C., Ogawa, T., and Egelman, E.H. (2001) Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA. Proc Natl Acad Sci USA 98: 8419-8424.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8419-8424
    • Yu, X.1    Jacobs, S.A.2    West, S.C.3    Ogawa, T.4    Egelman, E.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.