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Volumn 6, Issue 12, 1998, Pages 1553-1561

The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure for a putative ABC-type binding protein

Author keywords

ABC type binding protein; Metal binding protein; PsaA; Streptococcus pneumoniae

Indexed keywords

BACTERIA (MICROORGANISMS); NEGIBACTERIA; POSIBACTERIA; STREPTOCOCCUS; STREPTOCOCCUS PNEUMONIAE;

EID: 0032534754     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00153-1     Document Type: Article
Times cited : (188)

References (44)
  • 1
    • 0032020385 scopus 로고    scopus 로고
    • Novel pneumococcal surface proteins: Role in virulence and vaccine potential
    • Paton, J.C. (1998). Novel pneumococcal surface proteins: role in virulence and vaccine potential. Trends Microbiol. 6, 85-87.
    • (1998) Trends Microbiol. , vol.6 , pp. 85-87
    • Paton, J.C.1
  • 2
    • 0029846414 scopus 로고    scopus 로고
    • Sequence heterogeneity of PsaA, a 37-kilodalton putative adhesin essential for virulence of Streptococcus pneumoniae
    • Berry, A.M. & Paton, J.C. (1996). Sequence heterogeneity of PsaA, a 37-kilodalton putative adhesin essential for virulence of Streptococcus pneumoniae. Infect. Immun. 64, 5255-5262.
    • (1996) Infect. Immun. , vol.64 , pp. 5255-5262
    • Berry, A.M.1    Paton, J.C.2
  • 3
    • 0030894696 scopus 로고    scopus 로고
    • Limited diversity of Streptococcus pneumoniae psaA among pneumococcal vaccine serotypes
    • Sampson, J.S., Furlow, Z., Whitney, A.M., Williams, D., Facklam, R. & Carlone, G.M. (1997). Limited diversity of Streptococcus pneumoniae psaA among pneumococcal vaccine serotypes. Infect. Immun. 65, 1967-1971.
    • (1997) Infect. Immun. , vol.65 , pp. 1967-1971
    • Sampson, J.S.1    Furlow, Z.2    Whitney, A.M.3    Williams, D.4    Facklam, R.5    Carlone, G.M.6
  • 4
    • 0030200554 scopus 로고    scopus 로고
    • Protection of mice against fatal pneumococcal challenge by immunization with pneumococcal surface adhesin A (PsaA)
    • Talkington, D.F., Brown, B.G., Tharpe, J.A., Koening, A. & Russell, H. (1996). Protection of mice against fatal pneumococcal challenge by immunization with pneumococcal surface adhesin A (PsaA). Microb. Pathog. 2, 17-22.
    • (1996) Microb. Pathog. , vol.2 , pp. 17-22
    • Talkington, D.F.1    Brown, B.G.2    Tharpe, J.A.3    Koening, A.4    Russell, H.5
  • 5
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C.F. (1992). ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8, 67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 6
    • 0027256676 scopus 로고
    • Structural, functional and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam, R. & Saier, M.H., Jr. (1993). Structural, functional and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 57, 320-346.
    • (1993) Microbiol. Rev. , vol.57 , pp. 320-346
    • Tam, R.1    Saier Jr., M.H.2
  • 7
    • 0028987131 scopus 로고
    • Lipoproteins of Gram-positive bacteria
    • Sutcliffe, I.C. & Russell, R.R.B. (1995). Lipoproteins of Gram-positive bacteria. J. Bacteriol. 177, 1123-1128.
    • (1995) J. Bacteriol. , vol.177 , pp. 1123-1128
    • Sutcliffe, I.C.1    Russell, R.R.B.2
  • 8
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- and β-subunits from ATP synthase, myosin, kinases and other ATP requiring enzymes and a common nucleotide binding fold
    • Walker, J.E., Saraste, M., Runswick, M.J. & Gay, N.J. (1982). Distantly related sequences in the α- and β-subunits from ATP synthase, myosin, kinases and other ATP requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 9
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the Gram-positive bacterium Bacillus subtilis
    • Kunst, F., et al., & Danchin, A. (1997). The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. Nature 390, 249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Danchin, A.2
  • 10
    • 0030868591 scopus 로고    scopus 로고
    • Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases
    • Dintilhac, A., Alloing, G., Granadel, C. & Claverys, J.-P. (1997). Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases. Mol. Microbiol. 25, 727-739.
    • (1997) Mol. Microbiol. , vol.25 , pp. 727-739
    • Dintilhac, A.1    Alloing, G.2    Granadel, C.3    Claverys, J.-P.4
  • 11
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes
    • Quiocho, F.A. & Ledvina, P.S. (1996). Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes. Mol. Microbiol. 20, 17-25.
    • (1996) Mol. Microbiol. , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.S.2
  • 12
    • 0030691197 scopus 로고    scopus 로고
    • +3-binding protein reveals convergent evolution within a superfamily
    • +3-binding protein reveals convergent evolution within a superfamily. Nat. Struct. Biol. 4, 919-924.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 919-924
    • Bruns, C.M.1    McRee, D.E.2
  • 13
    • 0031228463 scopus 로고    scopus 로고
    • Crystal structure of the molybdate binding protein ModA
    • Hu, Y., Rech, S., Gunsalus, R.P. & Rees, D.C. (1997). Crystal structure of the molybdate binding protein ModA. Nat. Struct. Biol. 4, 703-707.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 703-707
    • Hu, Y.1    Rech, S.2    Gunsalus, R.P.3    Rees, D.C.4
  • 14
    • 0032212093 scopus 로고    scopus 로고
    • Expression, purification and preliminary X-ray crystallographic analysis of PsaA, a putative metal-transporter protein of Streptococcus pneumoniae
    • Pilling, P.A., Lawrence, M.C., Berry, A.M., Ogunniyi, A.D., Lock, R.A. & Paton, J.C. (1998). Expression, purification and preliminary X-ray crystallographic analysis of PsaA, a putative metal-transporter protein of Streptococcus pneumoniae. Acta Cryst. D 54, 1464-1466.
    • (1998) Acta Cryst. D , vol.54 , pp. 1464-1466
    • Pilling, P.A.1    Lawrence, M.C.2    Berry, A.M.3    Ogunniyi, A.D.4    Lock, R.A.5    Paton, J.C.6
  • 15
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & 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
  • 16
    • 0026734002 scopus 로고
    • Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii
    • Kim, J. & Rees, D.C. (1992). Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii. Nature 360, 553-560.
    • (1992) Nature , vol.360 , pp. 553-560
    • Kim, J.1    Rees, D.C.2
  • 17
    • 0025743329 scopus 로고
    • Sugar-binding and crystallographic studies of an arabinose-binding protein mutant (Met108Leu) that exhibits enhanced affinity and altered specificity
    • Vermersch, P.S., Lemon, D.D., Tesmer, J.J. & Quiocho, F.A. (1991). Sugar-binding and crystallographic studies of an arabinose-binding protein mutant (Met108Leu) that exhibits enhanced affinity and altered specificity. Biochemistry 30, 6861-6866.
    • (1991) Biochemistry , vol.30 , pp. 6861-6866
    • Vermersch, P.S.1    Lemon, D.D.2    Tesmer, J.J.3    Quiocho, F.A.4
  • 18
    • 0031933445 scopus 로고    scopus 로고
    • An ABC transporter system of Yersinia pestis allows utilization of chelated iron by Escherichia coli SAB11
    • Bearden, S.W., Staggs, T.M. & Perry, R.D. (1998). An ABC transporter system of Yersinia pestis allows utilization of chelated iron by Escherichia coli SAB11. J. Bacteriol. 180, 1135-1147.
    • (1998) J. Bacteriol. , vol.180 , pp. 1135-1147
    • Bearden, S.W.1    Staggs, T.M.2    Perry, R.D.3
  • 19
    • 0029027150 scopus 로고
    • Molecular identification of an ABC transporter complex for manganese: Analysis of a cyanobacterial mutant strain impaired in the photosynthetic oxygen evolution process
    • Bartsevich, V.V. & Pakrasi, H.B. (1995). Molecular identification of an ABC transporter complex for manganese: analysis of a cyanobacterial mutant strain impaired in the photosynthetic oxygen evolution process. EMBO J. 14, 1845-1853.
    • (1995) EMBO J. , vol.14 , pp. 1845-1853
    • Bartsevich, V.V.1    Pakrasi, H.B.2
  • 20
    • 0029175241 scopus 로고
    • Zinc metallochemistry in biochemistry
    • Jolies, P. & Jörnvall, H., eds Birkhäuser-Verlag, Basel
    • Vallee, B.L. & Auld, D.S. (1995). Zinc metallochemistry in biochemistry. In Interfaces between Chemistry and Biochemistry (Jolies, P. & Jörnvall, H., eds), pp. 259-277, Birkhäuser-Verlag, Basel.
    • (1995) Interfaces between Chemistry and Biochemistry , pp. 259-277
    • Vallee, B.L.1    Auld, D.S.2
  • 21
    • 0031473227 scopus 로고    scopus 로고
    • Structural chemistry and biology of manganese metalloenzymes
    • Christianson, D.W. (1997). Structural chemistry and biology of manganese metalloenzymes. Prog. Biophys. Mol. Biol. 67, 217-252.
    • (1997) Prog. Biophys. Mol. Biol. , vol.67 , pp. 217-252
    • Christianson, D.W.1
  • 22
    • 0021759355 scopus 로고
    • The crystal structure of poplar apoplastocyanin at 1.8 A resolution: The geometry of the copper-binding site is created by the polypeptide
    • Garrett, T.P.J., Clingeleffer, J., Guss, J.M., Rogers, S.J. & Freeman, H.C. (1984). The crystal structure of poplar apoplastocyanin at 1.8 A resolution: the geometry of the copper-binding site is created by the polypeptide. J. Biol. Chem. 259, 2822-2825.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2822-2825
    • Garrett, T.P.J.1    Clingeleffer, J.2    Guss, J.M.3    Rogers, S.J.4    Freeman, H.C.5
  • 23
    • 0019542603 scopus 로고
    • Surface components of Streptococcus pneumoniae
    • Tomasz, A. (1981). Surface components of Streptococcus pneumoniae. Rev. Infect. Dis. 3, 190-211.
    • (1981) Rev. Infect. Dis. , vol.3 , pp. 190-211
    • Tomasz, A.1
  • 24
    • 0028100391 scopus 로고
    • Nucleotide sequence of the Streptococcus gordonii PK488 coaggregation adhesin gene, scaA, and ATP-binding cassette
    • Kolenbrander, P.E., Andersen, R.N. & Ganeshkumar, N. (1994). Nucleotide sequence of the Streptococcus gordonii PK488 coaggregation adhesin gene, scaA, and ATP-binding cassette. Infect. Immun. 62, 4469-4480.
    • (1994) Infect. Immun. , vol.62 , pp. 4469-4480
    • Kolenbrander, P.E.1    Andersen, R.N.2    Ganeshkumar, N.3
  • 25
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 26
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavyatom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • Sweet, R.M. & Carter, C.W. Jr, eds Academic Press, New York
    • La Fortelle, E. de & Bricogne, G. (1997). Maximum-likelihood heavyatom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. In Methods in Enzymology 276. (Sweet, R.M. & Carter, C.W. Jr, eds), pp. 472-494, Academic Press, New York.
    • (1997) Methods in Enzymology , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 27
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams, J.P. & Leslie, A.G.W. (1996). Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Cryst. D 52, 30-42.
    • (1996) Acta Cryst. D , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 28
    • 0028158628 scopus 로고
    • PHD - An automatic mail server for protein secondary structure predictions
    • Rost, B., Sander, C. & Schneider, R. (1994). PHD - an automatic mail server for protein secondary structure predictions. Comput. Appl. Biosci. 10, 53-60.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 53-60
    • Rost, B.1    Sander, C.2    Schneider, R.3
  • 29
    • 0030931336 scopus 로고    scopus 로고
    • 75% accuracy in protein secondary structure prediction
    • Frischman, D. & Argos, P. (1997). 75% accuracy in protein secondary structure prediction. Proteins 27, 329-335.
    • (1997) Proteins , vol.27 , pp. 329-335
    • Frischman, D.1    Argos, P.2
  • 30
    • 0029804192 scopus 로고    scopus 로고
    • Identification and application of concepts important for accurate and reliable protein secondary structure prediction
    • King, R.D. & Sternberg, M.J.E. (1996). Identification and application of concepts important for accurate and reliable protein secondary structure prediction. Protein Sci. 5, 2298-2310.
    • (1996) Protein Sci. , vol.5 , pp. 2298-2310
    • King, R.D.1    Sternberg, M.J.E.2
  • 31
    • 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. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 32
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, J. & Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 33
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N., Vagin, A.A. & Dodson, E.J. (1997). Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst. D 53, 240-255.
    • (1997) Acta Cryst. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 34
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V.S. & Wilson, K.S. (1993). Automated refinement of protein models. Acta Cryst. D 49, 129-147.
    • (1993) Acta Cryst. D , vol.49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 35
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 36
    • 0030497978 scopus 로고    scopus 로고
    • Efficient rebuilding of protein structures
    • Kleywegt, G.J. & Jones, T.A. (1996). Efficient rebuilding of protein structures. Acta Cryst. D 52, 829-832.
    • (1996) Acta Cryst. D , vol.52 , pp. 829-832
    • Kleywegt, G.J.1    Jones, T.A.2
  • 37
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 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
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray structure refinement
    • Engh, R.A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray structure refinement. Acta Cryst. A 47, 392-400.
    • (1991) Acta Cryst. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 39
    • 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. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 40
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space-filling molecule pictures
    • Bacon, D. & Anderson, W.F. (1988). A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graph. 6, 219-220.
    • (1988) J. Mol. Graph. , vol.6 , pp. 219-220
    • Bacon, D.1    Anderson, W.F.2
  • 41
    • 0028057108 scopus 로고
    • Raster3D version 2.0 - A program for photorealistic molecular graphics
    • Merritt, E.A. & Murphy, M.E.P. (1994). Raster3D version 2.0 - a program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873.
    • (1994) Acta Cryst. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 42
    • 0027968068 scopus 로고
    • CLUSTALW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. & Gibson, T.J. (1994). CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acid Res., 22, 4673-4680.
    • (1994) Nucleic Acid Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 43
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. (1993). ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 44
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald, I.K. & Thornton, J.M. (1994). Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238, 777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2


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