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Volumn 345, Issue 4, 2005, Pages 879-892

The structure of the oligopeptide-binding protein, AppA, from Bacillus subtilis in complex with a nonapeptide

Author keywords

AppA; Bacillus subtilis; oligopeptide; transport; X ray crystallography

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATE; AMINO ACID; NONAPEPTIDE; OLIGOPEPTIDE;

EID: 10044241873     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.10.089     Document Type: Article
Times cited : (64)

References (60)
  • 1
    • 0019300651 scopus 로고
    • The number and nature of the peptide-transport systems of Escherichia coli: Characterization of specific transport mutants
    • R.A. Alves, and J.W. Payne The number and nature of the peptide-transport systems of Escherichia coli: characterization of specific transport mutants Biochem. Soc. Trans. 8 1980 704 705
    • (1980) Biochem. Soc. Trans. , vol.8 , pp. 704-705
    • Alves, R.A.1    Payne, J.W.2
  • 3
    • 0035823134 scopus 로고    scopus 로고
    • Structural biology. The xyz of ABC transporters
    • C.F. Higgins, and K.J. Linton Structural biology. The xyz of ABC transporters Science 293 2001 1782 1784
    • (2001) Science , vol.293 , pp. 1782-1784
    • Higgins, C.F.1    Linton, K.J.2
  • 5
    • 85067251635 scopus 로고    scopus 로고
    • Crystal structures of periplasmic solute binding proteins in ABC-transport complexes illuminate their function
    • I.B. Holland K. Kuchler C.F. Higgins S. Cole Academic Press London
    • A.J. Wilkinson, and K.H.G. Verschueren Crystal structures of periplasmic solute binding proteins in ABC-transport complexes illuminate their function I.B. Holland K. Kuchler C.F. Higgins S. Cole ABC Transporters from Bacteria to Man 2003 Academic Press London 187 208
    • (2003) ABC Transporters from Bacteria to Man , pp. 187-208
    • Wilkinson, A.J.1    Verschueren, K.H.G.2
  • 6
    • 0020478556 scopus 로고
    • Hinge-bending in l-arabinose-binding protein. The "venus's-fly- trap" model
    • B. Mao, M.R. Pear, J.A. McCammon, and F.A. Quiocho Hinge-bending in l-arabinose-binding protein. The "Venus's-fly-trap" model J. Biol. Chem. 257 1982 1131 1133
    • (1982) J. Biol. Chem. , vol.257 , pp. 1131-1133
    • Mao, B.1    Pear, M.R.2    McCammon, J.A.3    Quiocho, F.A.4
  • 7
  • 8
    • 0032806924 scopus 로고    scopus 로고
    • Relating structure to thermodynamics: The crystal structures and binding affinity of eight OppA-peptide complexes
    • T.G. Davies, R.E. Hubbard, and J.R. Tame Relating structure to thermodynamics: the crystal structures and binding affinity of eight OppA-peptide complexes Protein Sci. 8 1999 1432 1444
    • (1999) Protein Sci. , vol.8 , pp. 1432-1444
    • Davies, T.G.1    Hubbard, R.E.2    Tame, J.R.3
  • 9
    • 0034830834 scopus 로고    scopus 로고
    • The intracellular function of extracellular signaling peptides
    • B.A. Lazazzera The intracellular function of extracellular signaling peptides Peptides 22 2001 1519 1527
    • (2001) Peptides , vol.22 , pp. 1519-1527
    • Lazazzera, B.A.1
  • 10
    • 0026031219 scopus 로고
    • The oligopeptide transport system of Bacillus subtilis plays a role in the initiation of sporulation
    • M. Perego, C.F. Higgins, S.R. Pearce, M.P. Gallagher, and J.A. Hoch The oligopeptide transport system of Bacillus subtilis plays a role in the initiation of sporulation Mol. Microbiol. 5 1991 173 185
    • (1991) Mol. Microbiol. , vol.5 , pp. 173-185
    • Perego, M.1    Higgins, C.F.2    Pearce, S.R.3    Gallagher, M.P.4    Hoch, J.A.5
  • 11
    • 0025971265 scopus 로고
    • The spo0K locus of Bacillus subtilis is homologous to the oligopeptide permease locus and is required for sporulation and competence
    • D.Z. Rudner, J.R. LeDeaux, K. Ireton, and A.D. Grossman The spo0K locus of Bacillus subtilis is homologous to the oligopeptide permease locus and is required for sporulation and competence J. Bacteriol. 173 1991 1388 1398
    • (1991) J. Bacteriol. , vol.173 , pp. 1388-1398
    • Rudner, D.Z.1    Ledeaux, J.R.2    Ireton, K.3    Grossman, A.D.4
  • 12
    • 0027971083 scopus 로고
    • Identification of a second oligopeptide transport system in Bacillus subtilis and determination of its role in sporulation
    • A. Koide, and J.A. Hoch Identification of a second oligopeptide transport system in Bacillus subtilis and determination of its role in sporulation Mol. Microbiol. 13 1994 417 426
    • (1994) Mol. Microbiol. , vol.13 , pp. 417-426
    • Koide, A.1    Hoch, J.A.2
  • 14
    • 0028987131 scopus 로고
    • Lipoproteins of Gram-positive bacteria
    • I.C. Sutcliffe, and R.R. Russell Lipoproteins of Gram-positive bacteria J. Bacteriol. 177 1995 1123 1128
    • (1995) J. Bacteriol. , vol.177 , pp. 1123-1128
    • Sutcliffe, I.C.1    Russell, R.R.2
  • 15
    • 0024198129 scopus 로고
    • Evidence for high affinity binding-protein dependent transport systems in gram-positive bacteria and in mycoplasma
    • E. Gilson, G. Alloing, T. Schmidt, J.P. Claverys, R. Dudler, and M. Hofnung Evidence for high affinity binding-protein dependent transport systems in gram-positive bacteria and in mycoplasma EMBO J. 7 1988 3971 3974
    • (1988) EMBO J. , vol.7 , pp. 3971-3974
    • Gilson, E.1    Alloing, G.2    Schmidt, T.3    Claverys, J.P.4    Dudler, R.5    Hofnung, M.6
  • 16
    • 0030844587 scopus 로고    scopus 로고
    • A peptide export-import control circuit modulating bacterial development regulates protein phosphatases of the phosphorelay
    • M. Perego A peptide export-import control circuit modulating bacterial development regulates protein phosphatases of the phosphorelay Proc. Natl Acad. Sci. USA 94 1997 8612 8617
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 8612-8617
    • Perego, M.1
  • 17
    • 0034830557 scopus 로고    scopus 로고
    • Pentapeptide regulation of aspartyl-phosphate phosphatases
    • M. Perego, and J.A. Brannigan Pentapeptide regulation of aspartyl-phosphate phosphatases Peptides 22 2001 1541 1547
    • (2001) Peptides , vol.22 , pp. 1541-1547
    • Perego, M.1    Brannigan, J.A.2
  • 18
    • 0029959768 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular peptide factor that affects two different developmental pathways in Bacillus subtilis
    • J.M. Solomon, B.A. Lazazzera, and A.D. Grossman Purification and characterization of an extracellular peptide factor that affects two different developmental pathways in Bacillus subtilis Genes Dev. 10 1996 2014 2024
    • (1996) Genes Dev. , vol.10 , pp. 2014-2024
    • Solomon, J.M.1    Lazazzera, B.A.2    Grossman, A.D.3
  • 21
    • 0030855775 scopus 로고    scopus 로고
    • Peptide binding in OppA, the crystal structures of the periplasmic oligopeptide binding protein in the unliganded form and in complex with lysyllysine
    • S.H. Sleigh, J.R. Tame, E.J. Dodson, and A.J. Wilkinson Peptide binding in OppA, the crystal structures of the periplasmic oligopeptide binding protein in the unliganded form and in complex with lysyllysine Biochemistry 36 1997 9747 9758
    • (1997) Biochemistry , vol.36 , pp. 9747-9758
    • Sleigh, S.H.1    Tame, J.R.2    Dodson, E.J.3    Wilkinson, A.J.4
  • 23
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • L. Holm, and C. Sander Protein structure comparison by alignment of distance matrices J. Mol. Biol. 233 1993 123 138
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 24
    • 0028786979 scopus 로고
    • Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis
    • P. Dunten, and S.L. Mowbray Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis Protein Sci. 4 1995 2327 2334
    • (1995) Protein Sci. , vol.4 , pp. 2327-2334
    • Dunten, P.1    Mowbray, S.L.2
  • 25
    • 0029200246 scopus 로고
    • 2 Å resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor
    • A.V. Nickitenko, S. Trakhanov, and F.A. Quiocho 2 Å resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor Biochemistry 34 1995 16585 16595
    • (1995) Biochemistry , vol.34 , pp. 16585-16595
    • Nickitenko, A.V.1    Trakhanov, S.2    Quiocho, F.A.3
  • 26
    • 0346118916 scopus 로고    scopus 로고
    • Crystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coli
    • J. Heddle, D.J. Scott, S. Unzai, S.Y. Park, and J.R. Tame Crystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coli J. Biol. Chem. 278 2003 50322 50329
    • (2003) J. Biol. Chem. , vol.278 , pp. 50322-50329
    • Heddle, J.1    Scott, D.J.2    Unzai, S.3    Park, S.Y.4    Tame, J.R.5
  • 27
    • 0035019270 scopus 로고    scopus 로고
    • Peptide binding to the Bacillus subtilis oligopeptide-binding proteins OppA and AppA
    • A. Picon, and K.H.M. van Wely Peptide binding to the Bacillus subtilis oligopeptide-binding proteins OppA and AppA Mol. Biol. Today 2 2001 21 25
    • (2001) Mol. Biol. Today , vol.2 , pp. 21-25
    • Picon, A.1    Van Wely, K.H.M.2
  • 28
    • 0030044159 scopus 로고    scopus 로고
    • Enterococcus faecalis pheromone binding protein, PrgZ, recruits a chromosomal oligopeptide permease system to import sex pheromone cCF10 for induction of conjugation
    • B.A. Leonard, A. Podbielski, P.J. Hedberg, and G.M. Dunny Enterococcus faecalis pheromone binding protein, PrgZ, recruits a chromosomal oligopeptide permease system to import sex pheromone cCF10 for induction of conjugation Proc. Natl Acad. Sci. USA 93 1996 260 264
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 260-264
    • Leonard, B.A.1    Podbielski, A.2    Hedberg, P.J.3    Dunny, G.M.4
  • 29
    • 0033971943 scopus 로고    scopus 로고
    • Enterococcal sex pheromone precursors are part of signal sequences for surface lipoproteins
    • D.B. Clewell, F.Y. An, S.E. Flannagan, M. Antiporta, and G.M. Dunny Enterococcal sex pheromone precursors are part of signal sequences for surface lipoproteins Mol. Microbiol. 35 2000 246 247
    • (2000) Mol. Microbiol. , vol.35 , pp. 246-247
    • Clewell, D.B.1    An, F.Y.2    Flannagan, S.E.3    Antiporta, M.4    Dunny, G.M.5
  • 30
    • 0037256283 scopus 로고    scopus 로고
    • A plasmid-borne Rap-Phr system of Bacillus subtilis can mediate cell-density controlled production of extracellular proteases
    • E.J. Koetje, A. Hajdo-Milasinovic, R. Kiewiet, S. Bron, and H. Tjalsma A plasmid-borne Rap-Phr system of Bacillus subtilis can mediate cell-density controlled production of extracellular proteases Microbiology 149 2003 19 28
    • (2003) Microbiology , vol.149 , pp. 19-28
    • Koetje, E.J.1    Hajdo-Milasinovic, A.2    Kiewiet, R.3    Bron, S.4    Tjalsma, H.5
  • 31
    • 2442657883 scopus 로고    scopus 로고
    • Two oligopeptide-permease-encoding genes in the clavulanic acid cluster of Streptomyces clavuligerus are essential for production of the beta-lactamase inhibitor
    • L.M. Lorenzana, R. Perez-Redondo, I. Santamarta, J.F. Martin, and P. Liras Two oligopeptide-permease-encoding genes in the clavulanic acid cluster of Streptomyces clavuligerus are essential for production of the beta-lactamase inhibitor J. Bacteriol. 186 2004 3431 3438
    • (2004) J. Bacteriol. , vol.186 , pp. 3431-3438
    • Lorenzana, L.M.1    Perez-Redondo, R.2    Santamarta, I.3    Martin, J.F.4    Liras, P.5
  • 32
    • 0032564324 scopus 로고    scopus 로고
    • Kinetics and specificity of peptide uptake by the oligopeptide transport system of Lactococcus lactis
    • F.J. Detmers, E.R. Kunji, F.C. Lanfermeijer, B. Poolman, and W.N. Konings Kinetics and specificity of peptide uptake by the oligopeptide transport system of Lactococcus lactis Biochemistry 37 1998 16671 16679
    • (1998) Biochemistry , vol.37 , pp. 16671-16679
    • Detmers, F.J.1    Kunji, E.R.2    Lanfermeijer, F.C.3    Poolman, B.4    Konings, W.N.5
  • 33
    • 0033740174 scopus 로고    scopus 로고
    • Combinatorial peptide libraries reveal the ligand-binding mechanism of the oligopeptide receptor OppA of Lactococcus lactis
    • F.J. Detmers, F.C. Lanfermeijer, R. Abele, R.W. Jack, R. Tampe, W.N. Konings, and B. Poolman Combinatorial peptide libraries reveal the ligand-binding mechanism of the oligopeptide receptor OppA of Lactococcus lactis Proc. Natl Acad. Sci. USA 97 2000 12487 12492
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 12487-12492
    • Detmers, F.J.1    Lanfermeijer, F.C.2    Abele, R.3    Jack, R.W.4    Tampe, R.5    Konings, W.N.6    Poolman, B.7
  • 34
    • 3542996250 scopus 로고    scopus 로고
    • The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter
    • M.K. Doeven, R. Abele, R. Tampe, and B. Poolman The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter J. Biol. Chem. 279 2004 32301 32307
    • (2004) J. Biol. Chem. , vol.279 , pp. 32301-32307
    • Doeven, M.K.1    Abele, R.2    Tampe, R.3    Poolman, B.4
  • 35
    • 0029646113 scopus 로고
    • The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands
    • J.R. Tame, E.J. Dodson, G. Murshudov, C.F. Higgins, and A.J. Wilkinson The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands Structure 3 1995 1395 1406
    • (1995) Structure , vol.3 , pp. 1395-1406
    • Tame, J.R.1    Dodson, E.J.2    Murshudov, G.3    Higgins, C.F.4    Wilkinson, A.J.5
  • 36
    • 0345730812 scopus 로고    scopus 로고
    • Analysis of differences in the functional properties of the substrate binding proteins of the Borrelia burgdorferi oligopeptide permease (Opp) operon
    • X.G. Wang, J.M. Kidder, J.P. Scagliotti, M.S. Klempner, R. Noring, and L.T. Hu Analysis of differences in the functional properties of the substrate binding proteins of the Borrelia burgdorferi oligopeptide permease (Opp) operon J. Bacteriol. 186 2004 51 60
    • (2004) J. Bacteriol. , vol.186 , pp. 51-60
    • Wang, X.G.1    Kidder, J.M.2    Scagliotti, J.P.3    Klempner, M.S.4    Noring, R.5    Hu, L.T.6
  • 37
    • 0036842061 scopus 로고    scopus 로고
    • Effects of environmental changes on expression of the oligopeptide permease (opp) genes of Borrelia burgdorferi
    • X.G. Wang, B. Lin, J.M. Kidder, S. Telford, and L.T. Hu Effects of environmental changes on expression of the oligopeptide permease (opp) genes of Borrelia burgdorferi J. Bacteriol. 184 2002 6198 6206
    • (2002) J. Bacteriol. , vol.184 , pp. 6198-6206
    • Wang, X.G.1    Lin, B.2    Kidder, J.M.3    Telford, S.4    Hu, L.T.5
  • 38
    • 0034441194 scopus 로고    scopus 로고
    • OppA of Listeria monocytogenes, an oligopeptide-binding protein required for bacterial growth at low temperature and involved in intracellular survival
    • E. Borezee, E. Pellegrini, and P. Berche OppA of Listeria monocytogenes, an oligopeptide-binding protein required for bacterial growth at low temperature and involved in intracellular survival Infect. Immun. 68 2000 7069 7077
    • (2000) Infect. Immun. , vol.68 , pp. 7069-7077
    • Borezee, E.1    Pellegrini, E.2    Berche, P.3
  • 39
    • 3042685720 scopus 로고    scopus 로고
    • The Ami-AliA/AliB permease of Streptococcus pneumoniae is involved in nasopharyngeal colonization but not in invasive disease
    • A.R. Kerr, P.V. Adrian, S. Estevao, R. de Groot, G. Alloing, and J.P. Claverys The Ami-AliA/AliB permease of Streptococcus pneumoniae is involved in nasopharyngeal colonization but not in invasive disease Infect. Immun. 72 2004 3902 3906
    • (2004) Infect. Immun. , vol.72 , pp. 3902-3906
    • Kerr, A.R.1    Adrian, P.V.2    Estevao, S.3    De Groot, R.4    Alloing, G.5    Claverys, J.P.6
  • 40
    • 1342325449 scopus 로고    scopus 로고
    • Relevance of peptide uptake systems to the physiology and virulence of Streptococcus agalactiae
    • U. Samen, B. Gottschalk, B.J. Eikmanns, and D.J. Reinscheid Relevance of peptide uptake systems to the physiology and virulence of Streptococcus agalactiae J. Bacteriol. 186 2004 1398 1408
    • (2004) J. Bacteriol. , vol.186 , pp. 1398-1408
    • Samen, U.1    Gottschalk, B.2    Eikmanns, B.J.3    Reinscheid, D.J.4
  • 41
    • 0038752613 scopus 로고    scopus 로고
    • The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria
    • T.D. Read, S.N. Peterson, N. Tourasse, L.W. Baillie, I.T. Paulsen, and K.E. Nelson The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria Nature 423 2003 81 86
    • (2003) Nature , vol.423 , pp. 81-86
    • Read, T.D.1    Peterson, S.N.2    Tourasse, N.3    Baillie, L.W.4    Paulsen, I.T.5    Nelson, K.E.6
  • 42
    • 0035021910 scopus 로고    scopus 로고
    • Peptides and ATP binding cassette peptide transporters
    • F.J. Detmers, F.C. Lanfermeijer, and B. Poolman Peptides and ATP binding cassette peptide transporters Res. Microbiol. 152 2001 245 258
    • (2001) Res. Microbiol. , vol.152 , pp. 245-258
    • Detmers, F.J.1    Lanfermeijer, F.C.2    Poolman, B.3
  • 43
    • 0032985760 scopus 로고    scopus 로고
    • ScoC regulates peptide transport and sporulation initiation in Bacillus subtilis
    • A. Koide, M. Perego, and J.A. Hoch ScoC regulates peptide transport and sporulation initiation in Bacillus subtilis J. Bacteriol. 181 1999 4114 4117
    • (1999) J. Bacteriol. , vol.181 , pp. 4114-4117
    • Koide, A.1    Perego, M.2    Hoch, J.A.3
  • 44
    • 0035004349 scopus 로고    scopus 로고
    • Oligopeptide permease is required for expression of the Bacillus thuringiensis plcR regulon and for virulence
    • M. Gominet, L. Slamti, N. Gilois, M. Rose, and D. Lereclus Oligopeptide permease is required for expression of the Bacillus thuringiensis plcR regulon and for virulence Mol. Microbiol. 40 2001 963 975
    • (2001) Mol. Microbiol. , vol.40 , pp. 963-975
    • Gominet, M.1    Slamti, L.2    Gilois, N.3    Rose, M.4    Lereclus, D.5
  • 45
    • 0037009447 scopus 로고    scopus 로고
    • A cell-cell signaling peptide activates the PlcR virulence regulon in bacteria of the Bacillus cereus group
    • L. Slamti, and D. Lereclus A cell-cell signaling peptide activates the PlcR virulence regulon in bacteria of the Bacillus cereus group EMBO J. 21 2002 4550 4559
    • (2002) EMBO J. , vol.21 , pp. 4550-4559
    • Slamti, L.1    Lereclus, D.2
  • 46
    • 0021074501 scopus 로고
    • Periplasmic protein associated with the oligopeptide permeases of Salmonella typhimurium and Escherichia coli
    • C.F. Higgins, and M.M. Hardie Periplasmic protein associated with the oligopeptide permeases of Salmonella typhimurium and Escherichia coli J. Bacteriol. 155 1983 1434 1438
    • (1983) J. Bacteriol. , vol.155 , pp. 1434-1438
    • Higgins, C.F.1    Hardie, M.M.2
  • 47
    • 0031045818 scopus 로고    scopus 로고
    • Treatment of multiwavelength anomalous diffraction data as a special case of multiple isomorphous replacement
    • V. Ramakrishnan, and V. Biou Treatment of multiwavelength anomalous diffraction data as a special case of multiple isomorphous replacement Methods Enzymol. 276 1997 538 557
    • (1997) Methods Enzymol. , vol.276 , pp. 538-557
    • Ramakrishnan, V.1    Biou, V.2
  • 48
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Academic Press Inc., San Diego.
    • Otwinowski, Z. & Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. In Macromolecular Crystallography, Pt A, vol. 276, pp. 307-326, Academic Press Inc., San Diego.
    • (1997) Macromolecular Crystallography, Pt A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 49
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • Leslie, A. G. W. (1992). Recent changes to the MOSFLM package for processing film and image plate data. Jnt CCP4/ESF-EACMB Newslett. Protein Crystallog. No. 26.
    • (1992) Jnt CCP4/ESF-EACMB Newslett. Protein Crystallog. , vol.26
    • Leslie, A.G.W.1
  • 50
    • 0035788131 scopus 로고    scopus 로고
    • Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps
    • A.A. Vagin, and M.N. Isupov Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps Acta Crystallog. sect. D 57 2001 1451 1456
    • (2001) Acta Crystallog. Sect. D , vol.57 , pp. 1451-1456
    • Vagin, A.A.1    Isupov, M.N.2
  • 53
    • 0002583957 scopus 로고
    • DM, an automated procedure for phase improvement by density modification
    • K. Cowtan DM, an automated procedure for phase improvement by density modification Jnt CCP4/ESF-EACBM Newslett. Protein Crystallog. 31 1994 24 28
    • (1994) Jnt CCP4/ESF-EACBM Newslett. Protein Crystallog. , vol.31 , pp. 24-28
    • Cowtan, K.1
  • 54
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallog. sect. D 53 1997 240 255
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 55
    • 0036075042 scopus 로고    scopus 로고
    • High-resolution crystallographic map interpretation
    • T.J. Oldfield High-resolution crystallographic map interpretation Acta Crystallog. sect. D 58 2002 963 967
    • (2002) Acta Crystallog. Sect. D , vol.58 , pp. 963-967
    • Oldfield, T.J.1
  • 56
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • A. Perrakis, R. Morris, and V.S. Lamzin Automated protein model building combined with iterative structure refinement Nature Struct. Biol. 6 1999 458 463
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 57
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • M.D. Winn, M.N. Isupov, and G.N. Murshudov Use of TLS parameters to model anisotropic displacements in macromolecular refinement Acta Crystallog. sect. D 57 2001 122 133
    • (2001) Acta Crystallog. Sect. D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 58
    • 0025964291 scopus 로고
    • Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay
    • D. Burbulys, K.A. Trach, and J.A. Hoch Initiation of sporulation in B. 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
  • 59
    • 0026244229 scopus 로고
    • MOLSCRIPT - A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT - a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 60
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • E.A. Merritt, and D.J. Bacon Raster3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.