메뉴 건너뛰기




Volumn 18, Issue 16, 1999, Pages 4513-4522

X-ray structure of aminopeptidase A from Escherichia coli and a model for the nucleoprotein complex in Xer site-specific recombination

Author keywords

DNA looping; DNA binding proteins; Protein crystallography; Protein protein complexes; Site specific recombination

Indexed keywords

BACTERIAL ENZYME; CYTOSOL AMINOPEPTIDASE; DNA BINDING PROTEIN; GLUTAMYL AMINOPEPTIDASE; NUCLEOPROTEIN; REPRESSOR PROTEIN;

EID: 0344931801     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.16.4513     Document Type: Article
Times cited : (101)

References (37)
  • 1
    • 0342618313 scopus 로고    scopus 로고
    • Direct interaction of aminopeptidase A with recombination site DNA in Xer site-specific recombination
    • Alén, C., Sherratt, D.J. and Colloms, S.D. (1997) Direct interaction of aminopeptidase A with recombination site DNA in Xer site-specific recombination. EMBO J., 16, 5188-5197.
    • (1997) EMBO J. , vol.16 , pp. 5188-5197
    • Alén, C.1    Sherratt, D.J.2    Colloms, S.D.3
  • 2
    • 0027422093 scopus 로고
    • Two related recombinases are required for site-specific recombination at dif and cer in Escherichia coli K12
    • Blakely, G., May, G., McCulloch, R., Arciszewska, L., Burke, M., Lovett, S. and Sherratt, D.J. (1993) Two related recombinases are required for site-specific recombination at dif and cer in Escherichia coli K12. Cell, 75, 351-361.
    • (1993) Cell , vol.75 , pp. 351-361
    • Blakely, G.1    May, G.2    McCulloch, R.3    Arciszewska, L.4    Burke, M.5    Lovett, S.6    Sherratt, D.J.7
  • 3
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger, A.T. et al. (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr., D54, 905-921.
    • (1998) Acta Crystallogr. , vol.D54 , pp. 905-921
    • Brünger, A.T.1
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr., D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 6
    • 0029146877 scopus 로고
    • carP, involved in pyrimidine regulation of the Escherichia coli carbamoylphosphate synthetase operon encodes a sequence-specific DNA-binding protein identical to XerB and PepA, also required for resolution of ColE1 multimers
    • Charlier, D., Hassanzadeh, G., Kholti, A., Gigot, D., Piérard, A. and Glansdorff, N. (1995) carP, involved in pyrimidine regulation of the Escherichia coli carbamoylphosphate synthetase operon encodes a sequence-specific DNA-binding protein identical to XerB and PepA, also required for resolution of ColE1 multimers. J. Mol. Biol., 250, 392-406.
    • (1995) J. Mol. Biol. , vol.250 , pp. 392-406
    • Charlier, D.1    Hassanzadeh, G.2    Kholti, A.3    Gigot, D.4    Piérard, A.5    Glansdorff, N.6
  • 7
    • 0025602270 scopus 로고
    • Recombination at ColE1 cer requires the escherichia coli xerC gene product, a member of the λ integrase family of site-specific recombinases
    • Colloms, S.D., Sykora, P., Szatmari, G. and Sherratt, D.J. (1990) Recombination at ColE1 cer requires the Escherichia coli xerC gene product, a member of the λ integrase family of site-specific recombinases. J. Bacteriol., 172, 6973-6980.
    • (1990) J. Bacteriol. , vol.172 , pp. 6973-6980
    • Colloms, S.D.1    Sykora, P.2    Szatmari, G.3    Sherratt, D.J.4
  • 9
    • 0030943173 scopus 로고    scopus 로고
    • Topological selectivity in Xer site-specific recombination
    • Colloms, S.D., Bath, J. and Sherratt, D.J. (1997) Topological selectivity in Xer site-specific recombination. Cell, 88, 855-864.
    • (1997) Cell , vol.88 , pp. 855-864
    • Colloms, S.D.1    Bath, J.2    Sherratt, D.J.3
  • 10
    • 84988087911 scopus 로고
    • Calculating the electrostatic potential of molecules in solution: Method and error assessment
    • Gilson, M.K., Sharp, K.A. and Honig, B.H. (1987) Calculating the electrostatic potential of molecules in solution: method and error assessment. J. Comp. Chem., 9, 327-335.
    • (1987) J. Comp. Chem. , vol.9 , pp. 327-335
    • Gilson, M.K.1    Sharp, K.A.2    Honig, B.H.3
  • 11
    • 0032528271 scopus 로고    scopus 로고
    • Structure of the holliday junction intermediate in Cre-lox P site-specific recombination
    • Gopaul, D.N., Guo, F. and van Duyne, G.D. (1998) Structure of the Holliday junction intermediate in Cre-lox P site-specific recombination. EMBO J., 17, 4175-4187.
    • (1998) EMBO J. , vol.17 , pp. 4175-4187
    • Gopaul, D.N.1    Guo, F.2    Van Duyne, G.D.3
  • 12
    • 0030669944 scopus 로고    scopus 로고
    • Insertion mutagenesis as a tool in the modification of protein function. Extended substrate specificity conferred by pentapeptide insertions in the omega-loop of TEM-1 β-lactamase
    • Hayes, F., Hallet, B. and Cao, Y. (1997) Insertion mutagenesis as a tool in the modification of protein function. Extended substrate specificity conferred by pentapeptide insertions in the omega-loop of TEM-1 β-lactamase. J. Biol. Chem., 272, 28833-28836.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28833-28836
    • Hayes, F.1    Hallet, B.2    Cao, Y.3
  • 13
    • 0031872788 scopus 로고    scopus 로고
    • Nucleoprotein architecture and ColE1 dimer resolution: A hypothesis
    • Hodgman, T.C., Griffiths, H. and Summers, D.K. (1998) Nucleoprotein architecture and ColE1 dimer resolution: a hypothesis. Mol. Microbiol., 29, 545-558.
    • (1998) Mol. Microbiol. , vol.29 , pp. 545-558
    • Hodgman, T.C.1    Griffiths, H.2    Summers, D.K.3
  • 14
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol., 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 15
    • 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. Acta Crystallogr., A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 16
    • 0032563126 scopus 로고    scopus 로고
    • pyrH-encoded UMP-kinase directly participates in pyrimidine-specific modulation of promoter activity in Escherichia coli
    • Kholti, A., Charlier, D., Gigot, D., Huysveld, N., Roovers, M. and Glansdorff, N. (1998) pyrH-encoded UMP-kinase directly participates in pyrimidine-specific modulation of promoter activity in Escherichia coli. J. Mol. Biol. 280, 571-582.
    • (1998) J. Mol. Biol. , vol.280 , pp. 571-582
    • Kholti, A.1    Charlier, D.2    Gigot, D.3    Huysveld, N.4    Roovers, M.5    Glansdorff, N.6
  • 17
    • 0028045722 scopus 로고
    • Structure and mechanism of bovine lens leucine aminopeptidase
    • Kim, H. and Lipscomb, W.N. (1994) Structure and mechanism of bovine lens leucine aminopeptidase. Adv. Enzymol., 68, 153-213.
    • (1994) Adv. Enzymol. , vol.68 , pp. 153-213
    • Kim, H.1    Lipscomb, W.N.2
  • 18
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (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.J.1
  • 19
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K., Mäder, A.W., Richmond, R.K., Sargent, D.F. and Richmond, T.J. (1997) Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature, 389, 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 20
    • 0345983583 scopus 로고    scopus 로고
    • Modeling unusual nucleic acid structures
    • Leontes, N.B. and SantaLucia, J. (eds), American Chemical Society, Washington, DC
    • Macke, T. and Case, D.A. (1998) Modeling unusual nucleic acid structures. In Leontes, N.B. and SantaLucia, J. (eds), Molecular Modeling of Nucleic Acids. American Chemical Society, Washington, DC, pp.379-393.
    • (1998) Molecular Modeling of Nucleic Acids , pp. 379-393
    • Macke, T.1    Case, D.A.2
  • 21
    • 0028237249 scopus 로고
    • Peptidase activity of Escherichia coli aminopeptidase A is not required for its role in Xer site-specific recombination
    • McCulloch, R., Burke, M.E. and Sherratt, D.J. (1994) Peptidase activity of Escherichia coli aminopeptidase A is not required for its role in Xer site-specific recombination. Mol. Microbiol, 12, 241-251.
    • (1994) Mol. Microbiol , vol.12 , pp. 241-251
    • McCulloch, R.1    Burke, M.E.2    Sherratt, D.J.3
  • 22
    • 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
  • 23
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994) AMoRe: an automated package for molecular replacement. Acta Crystallogr., A50, 157-163.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 25
    • 0026319199 scopus 로고
    • Protein folding and association; insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. and Honig, B.H. (1991) Protein folding and association; insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins, 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.H.3
  • 27
    • 0028209323 scopus 로고
    • Model for a DNA-mediated synaptic complex suggested by crystal packing of γδ resolvase subunits
    • Rice, P.A. and Steitz, T.A. (1994) Model for a DNA-mediated synaptic complex suggested by crystal packing of γδ resolvase subunits. EMBO J., 13, 1514-1524.
    • (1994) EMBO J. , vol.13 , pp. 1514-1524
    • Rice, P.A.1    Steitz, T.A.2
  • 28
    • 0024293535 scopus 로고
    • The arginine represser is essential for plasmid-stabilising site-specific recombination at the ColE1 cer locus
    • Stirling, C.J., Szatmari, G., Stewart, G., Smith, M.C.M. and Sherratt, D.J. (1988) The arginine represser is essential for plasmid-stabilising site-specific recombination at the ColE1 cer locus. EMBO J., 7, 4389-4395.
    • (1988) EMBO J. , vol.7 , pp. 4389-4395
    • Stirling, C.J.1    Szatmari, G.2    Stewart, G.3    Smith, M.C.M.4    Sherratt, D.J.5
  • 29
    • 0024316734 scopus 로고
    • xerB, an Escherichia coli gene required for plasmid ColE1 site-specific recombination, is identical to pepA, encoding aminopeptidase A, a protein with substantial similarity to bovine lens leucine aminopeptidase
    • Stirling, C.J., Colloms, S.D., Collins, J.F., Szatmari, G. and Sherratt, D.J. (1989) xerB, an Escherichia coli gene required for plasmid ColE1 site-specific recombination, is identical to pepA, encoding aminopeptidase A, a protein with substantial similarity to bovine lens leucine aminopeptidase. EMBO J., 8, 1623-1627.
    • (1989) EMBO J. , vol.8 , pp. 1623-1627
    • Stirling, C.J.1    Colloms, S.D.2    Collins, J.F.3    Szatmari, G.4    Sherratt, D.J.5
  • 30
    • 0028889561 scopus 로고
    • Two-metal ion mechanism of bovine lens leucine aminopeptidase: Active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography
    • Sträter, N. and Lipscomb, W.N. (1995a) Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography. Biochemistry, 34, 14792-14800.
    • (1995) Biochemistry , vol.34 , pp. 14792-14800
    • Sträter, N.1    Lipscomb, W.N.2
  • 31
    • 0029116127 scopus 로고
    • Transition state analogue L-leucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 Å resolution in a new crystal form
    • Sträter, N. and Lipscomb, W.N. (1995b) Transition state analogue L-leucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 Å resolution in a new crystal form. Biochemistry, 34, 9200-9210.
    • (1995) Biochemistry , vol.34 , pp. 9200-9210
    • Sträter, N.1    Lipscomb, W.N.2
  • 32
    • 0039912678 scopus 로고    scopus 로고
    • Leucyl aminopeptidase (animal and plant)
    • Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (eds), Academic Press, New York, NY
    • Sträter, N. and Lipscomb, W.N. (1998) Leucyl aminopeptidase (animal and plant). In Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (eds), Handbook of Proteolytic Enzymes. Academic Press, New York, NY, pp. 1384-1389.
    • (1998) Handbook of Proteolytic Enzymes , pp. 1384-1389
    • Sträter, N.1    Lipscomb, W.N.2
  • 34
    • 0021419102 scopus 로고
    • Multimerisation of high copy number plasmids causes instability: ColE1 encodes a determinant for plasmid monomerisation and stability
    • Summers, D.K. and Sherratt, D.J. (1984) Multimerisation of high copy number plasmids causes instability: ColE1 encodes a determinant for plasmid monomerisation and stability. Cell, 36, 1097-1103.
    • (1984) Cell , vol.36 , pp. 1097-1103
    • Summers, D.K.1    Sherratt, D.J.2
  • 35
    • 0030880717 scopus 로고    scopus 로고
    • Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA
    • Sunnerhagen, M., Nilges, M., Otting, G. and Carey, J. (1997) Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA. Nature Struct. Biol., 4, 819-826.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 819-826
    • Sunnerhagen, M.1    Nilges, M.2    Otting, G.3    Carey, J.4
  • 36
    • 0029670095 scopus 로고    scopus 로고
    • Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli
    • van Duyne, G.D., Ghosh, G., Maas, W.K. and Sigler, P.B. (1996) Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli. J. Mol. Biol., 256, 377-391.
    • (1996) J. Mol. Biol. , vol.256 , pp. 377-391
    • Van Duyne, G.D.1    Ghosh, G.2    Maas, W.K.3    Sigler, P.B.4
  • 37
    • 0014962699 scopus 로고
    • Purification and properties of an aminopeptidase from Escherichia coli
    • Vogt, V.M. (1970) Purification and properties of an aminopeptidase from Escherichia coli. J. Biol. Chem., 245, 4760-4769.
    • (1970) J. Biol. Chem. , vol.245 , pp. 4760-4769
    • Vogt, V.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.