메뉴 건너뛰기




Volumn 33, Issue 5, 2005, Pages 1465-1473

Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; DOUBLE STRANDED DNA; RAD51 PROTEIN; RADA PROTEIN; RECA PROTEIN; RECOMBINASE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG; ARCHAEAL PROTEIN; DNA BINDING PROTEIN; RAD51 PROTEIN, HUMAN; RADA PROTEIN, ARCHAEAL;

EID: 14844355639     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gki288     Document Type: Article
Times cited : (30)

References (44)
  • 1
    • 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. [i#Front. Biosci.#1i], [b#3#1b], D570-D603.
    • (1998) Front. Biosci. , vol.3
    • Bianco, P.R.1    Tracy, R.B.2    Kowalczykowski, S.C.3
  • 2
    • 0035997347 scopus 로고    scopus 로고
    • The bacterial RecA protein and the recombinational DNA repair of stalled replication forks
    • Lusetti,S.L. and Cox,M.M. (2002) The bacterial RecA protein and the recombinational DNA repair of stalled replication forks. [i#Annu. Rev. Biochem.#1i], [b#71#1b], 71-100.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 71-100
    • Lusetti, S.L.1    Cox, M.M.2
  • 3
    • 0038202108 scopus 로고    scopus 로고
    • Archaeal DNA repair: Paradigms and puzzles
    • White,M.F. (2003) Archaeal DNA repair: Paradigms and puzzles. [i#Biochem. Soc. Trans.#1i], [b#31#1b], 690-693.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 690-693
    • White, M.F.1
  • 4
    • 0032079749 scopus 로고    scopus 로고
    • RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange
    • Seitz,E.M., Brockman,J.P., Sandler,S.J., Clark,A.J. and Kowalczykowski,S.C. (1998) RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange. [i#Genes Dev.#1i], [b#12#1b], 1248-1253.
    • (1998) Genes Dev. , vol.12 , pp. 1248-1253
    • Seitz, E.M.1    Brockman, J.P.2    Sandler, S.J.3    Clark, A.J.4    Kowalczykowski, S.C.5
  • 5
    • 0034721873 scopus 로고    scopus 로고
    • Domain analysis of an archaeal RadA protein for the strand exchange activity
    • Komori,K., Miyata,T., Daiyasu,H., Toh,H., Shinagawa,H. and Ishino,Y. (2000) Domain analysis of an archaeal RadA protein for the strand exchange activity. [i#J. Biol. Chem.#1i], [b#275#1b], 33791-33797.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33791-33797
    • Komori, K.1    Miyata, T.2    Daiyasu, H.3    Toh, H.4    Shinagawa, H.5    Ishino, Y.6
  • 6
    • 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. [i#J. Mol. Biol.#1i], [b#290#1b], 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
  • 7
    • 0023008741 scopus 로고
    • Structure of helical RecA-DNA complexes. Complexes formed in the presence of ATP-gamma-S or ATP
    • Egelman,E.H. and Stasiak,A. (1986) Structure of helical RecA-DNA complexes. Complexes formed in the presence of ATP-gamma-S or ATP. [i#J. Mol. Biol.#1i], [b#191#1b], 677-697.
    • (1986) J. Mol. Biol. , vol.191 , pp. 677-697
    • Egelman, E.H.1    Stasiak, A.2
  • 8
    • 0026666652 scopus 로고
    • Structural data suggest that the active and inactive forms of the RecA filament are not simply interconvertible
    • Yu,X. and Egelman,E.H. (1992) Structural data suggest that the active and inactive forms of the RecA filament are not simply interconvertible. [i#J. Mol. Biol.#1i], [b#227#1b], 334-346.
    • (1992) J. Mol. Biol. , vol.227 , pp. 334-346
    • Yu, X.1    Egelman, E.H.2
  • 9
    • 0034671684 scopus 로고    scopus 로고
    • Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AIF(4): Implications for decreased ATPase activity and molecular aggregation
    • Datta,S., Prabu,M.M., Vaze,M.B., Ganesh,N., Chandra,N.R., Muniyappa,K. and Vijayan,M. (2000) Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AIF(4): Implications for decreased ATPase activity and molecular aggregation. [i#Nucleic Acids Res.#1i], [b#28#1b], 4964-4973.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 4964-4973
    • Datta, S.1    Prabu, M.M.2    Vaze, M.B.3    Ganesh, N.4    Chandra, N.R.5    Muniyappa, K.6    Vijayan, M.7
  • 10
    • 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. (2003) Crystal structures of [i#Mycobacterium smegmatis#1i] RecA and its nucleotide complexes. [i#J. Bacteriol.#1i], [b#185#1b], 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
  • 11
    • 4444308700 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli RecA in a compressed helical filament
    • Xing,X. and Bell,C.E. (2004) Crystal structures of [i#Escherichia coli#1i] RecA in a compressed helical filament. [i#J. Mol. Biol.#1i], [b#342#1b] 1471-1485.
    • (2004) J. Mol. Biol. , vol.342 , pp. 1471-1485
    • Xing, X.1    Bell, C.E.2
  • 12
    • 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 [i#Deinococcus radiodurans#1i]: Insights into the structural basis of extreme radioresistance. [i#J. Mol. Biol.#1i], [b#344#1b], 951-963.
    • (2004) J. Mol. Biol. , vol.344 , pp. 951-963
    • Rajan, R.1    Bell, C.E.2
  • 13
    • 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 [i#E.coli#1i] recA protein monomer and polymer. [i#Nature#1i], [b#355#1b], 318-325.
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 14
    • 0031013231 scopus 로고    scopus 로고
    • The RecA hexamer is a structural homologue of ring helicases
    • Yu,X. and Egelman,E.H. (1997) The RecA hexamer is a structural homologue of ring helicases. [i#Nature Struct. Biol.#1i], [b#4#1b], 101-104.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 101-104
    • Yu, X.1    Egelman, E.H.2
  • 16
    • 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. [i#Proc. Natl Acad. Sci. USA#1i], [b#98#1b], 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
  • 18
    • 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., Kurumizaka,H. and Yokoyama,S. (2004) Structural basis for octameric ring formation and DNA interaction of the human homologous-pairing protein Dmc1. [i#Mol. Cell#1i], [b#14#1b], 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    Kurumizaka, H.7    Yokoyama, S.8
  • 19
    • 2642537689 scopus 로고    scopus 로고
    • Human meiotic recombinase Dmc1 promotes ATP-dependent homologous DNA strand exchange
    • Sehorn,M.G., Sigurdsson,S., Bussen,W., Unger,V.M. and Sung,P. (2004) Human meiotic recombinase Dmc1 promotes ATP-dependent homologous DNA strand exchange. [i#Nature#1i], [b#429#1b], 433-437.
    • (2004) Nature , vol.429 , pp. 433-437
    • Sehorn, M.G.1    Sigurdsson, S.2    Bussen, W.3    Unger, V.M.4    Sung, P.5
  • 20
    • 0035890601 scopus 로고    scopus 로고
    • RadA protein from Archaeoglobus fulgidus forms rings, nucleoprotein filaments and catalyses homologous recombination
    • McIlwraith,M.J., Hall,D.R., Stasiak,A.Z., Stasiak,A., Wigley,D.B. and West,S.C. (2001) RadA protein from [i#Archaeoglobus fulgidus#1i] forms rings, nucleoprotein filaments and catalyses homologous recombination. [i#Nucleic Acids Res.#1i], [b#29#1b], 4509-4517.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 4509-4517
    • McIlwraith, M.J.1    Hall, D.R.2    Stasiak, A.Z.3    Stasiak, A.4    Wigley, D.B.5    West, S.C.6
  • 21
    • 0035861994 scopus 로고    scopus 로고
    • Archaeal RadA protein binds DNA as both helical filaments and octameric rings
    • Yang,S., Yu,X., Seitz,E.M., Kowalczykowski,S.C. and Egelman,E.H. (2001) Archaeal RadA protein binds DNA as both helical filaments and octameric rings. [i#J. Mol. Biol.#1i], [b#314#1b], 1077-1085.
    • (2001) J. Mol. Biol. , vol.314 , pp. 1077-1085
    • Yang, S.1    Yu, X.2    Seitz, E.M.3    Kowalczykowski, S.C.4    Egelman, E.H.5
  • 22
    • 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. [i#Mol. Cell#1i], [b#15#1b], 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
  • 24
    • 3242886313 scopus 로고    scopus 로고
    • Homologous recombination-mediated double-strand break repair
    • Wyman,C., Ristic,D. and Kanaar,R. (2004) Homologous recombination-mediated double-strand break repair. [i#DNA Repair (Amst. #1i] [b#3#1b], 827-833.
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 827-833
    • Wyman, C.1    Ristic, D.2    Kanaar, R.3
  • 25
    • 2242443513 scopus 로고    scopus 로고
    • Insights into DNA recombination from the structure of a Rad51-BRCA2 complex
    • Pellegrini,L., Yu,D.S., Lo,T., Anand,S., Lee,M., Blundell,T.L. and Venkitaraman,A.R. (2002) Insights into DNA recombination from the structure of a Rad51-BRCA2 complex. [i#Nature#1i], [b#420#1b], 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    Venkitaraman, A.R.7
  • 27
    • 1242275403 scopus 로고    scopus 로고
    • Domain mapping of the Rad51 paralog protein complexes
    • Miller,K.A., Sawicka,D., Barsky,D. and Albala,J.S. (2004) Domain mapping of the Rad51 paralog protein complexes. [i#Nucleic Acids Res.#1i], [b#32#1b] 169-178.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 169-178
    • Miller, K.A.1    Sawicka, D.2    Barsky, D.3    Albala, J.S.4
  • 28
    • 0346340054 scopus 로고    scopus 로고
    • Rad51C is required for Holliday junction processing in mammalian cells
    • Liu,Y., Masson,J.Y., Shah,R., O'Regan,P. and West,S.C. (2004) Rad51C is required for Holliday junction processing in mammalian cells. [i#Science#1i] [b#303#1b], 243-246.
    • (2004) Science , vol.303 , pp. 243-246
    • Liu, Y.1    Masson, J.Y.2    Shah, R.3    O'Regan, P.4    West, S.C.5
  • 30
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews,B.W. (1968) Solvent content of protein crystals. [i#J. Mol. Biol.#1i], [b#33#1b], 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 31
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project,N
    • Collaborative Computational Project,N. (1994), The CCP4 suite: Programs for protein crystallography. [i#Acta Crystallogr. D Biol. Crystallogr.#1i] [b#50#1b], 760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 33
    • 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. and Kjeldgaard,M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. [i#Acta Crystallogr. A#1i], [b#47#1b], 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 34
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley,P. and Cowtan,K. (2004) Coot: Model-building tools for molecular graphics. [i#Acta Crystallogr. D Biol. Crystallogr.#1i], [b#60#1b], 2126-2132.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 36
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski,R.A., MacArthur,M.W., Moss,D.S. and Thornton,J.M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures. [i#J. Appl. Cryst.#1i], [b#26#1b], 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 38
    • 0030841589 scopus 로고    scopus 로고
    • Detecting fold motifs and similarities in protein structures
    • Kleywegt,G.J. and Jones,T.A. (1997) Detecting fold motifs and similarities in protein structures. [i#Methods Enzymol.#1i], [b#277#1b], 525-545.
    • (1997) Methods Enzymol. , vol.277 , pp. 525-545
    • Kleywegt, G.J.1    Jones, T.A.2
  • 39
    • 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. [i#Nature#1i], [b#355#1b], 374-376.
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 40
    • 0016771835 scopus 로고
    • Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2
    • Perutz,M.F. and Raidt,H. (1975) Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2. [i#Nature#1i], [b#255#1b], 256-259.
    • (1975) Nature , vol.255 , pp. 256-259
    • Perutz, M.F.1    Raidt, H.2
  • 41
    • 0036931447 scopus 로고    scopus 로고
    • Toward the physical basis of thermophilic proteins: Linking of enriched polar interactions and reduced heat capacity of unfolding
    • Zhou,H.X. (2002) Toward the physical basis of thermophilic proteins: linking of enriched polar interactions and reduced heat capacity of unfolding. [i#Biophys. J.#1i], [b#93#1b], 3126-3133.
    • (2002) Biophys. J. , vol.93 , pp. 3126-3133
    • Zhou, H.X.1
  • 42
    • 0037250158 scopus 로고    scopus 로고
    • InterpreTS: Protein interaction prediction through tertiary structure
    • Aloy,P. and Russell,R.B. (2003) InterpreTS: Protein interaction prediction through tertiary structure. [i#Bioinformatics#1i], [b#19#1b], 161-162.
    • (2003) Bioinformatics , vol.19 , pp. 161-162
    • Aloy, P.1    Russell, R.B.2
  • 44
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch,W. and Sander,C. (1983) Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. [i#Biopolymers#1i], [b#22#1b], 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.