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Volumn 487, Issue 7405, 2012, Pages 119-122

SbsB structure and lattice reconstruction unveil Ca2+ triggered S-layer assembly

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CALCIUM; IMMUNOGLOBULIN; MEMBRANE PROTEIN; NANOMATERIAL; SBSB PROTEIN, BACILLUS STEAROTHERMOPHILUS; CALCIUM ION; MONOMER; SBSB PROTEIN; UNCLASSIFIED DRUG;

EID: 84863497306     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature11155     Document Type: Letter
Times cited : (115)

References (47)
  • 2
    • 73049177078 scopus 로고
    • The fine structure of bacteria
    • Glauert, A. M. The fine structure of bacteria. Br. Med. Bull. 18, 245-250 (1962).
    • (1962) Br. Med. Bull. , pp. 245-250
    • Glauert, A.M.1
  • 5
    • 79960969172 scopus 로고    scopus 로고
    • Rationally engineering natural protein assemblies in nanobiotechnology
    • Howorka, S. Rationally engineering natural protein assemblies in nanobiotechnology. Curr. Opin. Biotechnol. 22, 485-491 (2011).
    • (2011) Curr. Opin. Biotechnol. , pp. 485-491
    • Howorka, S.1
  • 6
    • 33646369372 scopus 로고    scopus 로고
    • Bionanofabrication of metallic and semiconductor nanoparticle arrays using S-layer protein lattices with different lateral spacings and geometries
    • Mark, S.S. etal. Bionanofabrication of metallic and semiconductor nanoparticle arrays using S-layer protein lattices with different lateral spacings and geometries. Langmuir 22, 3763-3774 (2006).
    • (2006) Langmuir , pp. 3763-3774
    • Mark, S.S.1
  • 7
    • 77952251717 scopus 로고    scopus 로고
    • Biologically templated photocatalytic nanostructures for sustained light-driven water oxidation
    • Nam, Y.S. etal. Biologically templated photocatalytic nanostructures for sustained light-driven water oxidation. Nature Nanotechnol. 5, 340-344 (2010).
    • (2010) Nature Nanotechnol. , vol.5 , pp. 340-344
    • Nam, Y.S.1
  • 8
    • 60649099858 scopus 로고    scopus 로고
    • Structural insights into the molecular organization of the S-layer from
    • Fagan, R. P. etal. Structural insights into the molecular organization of the S-layer from Clostridium difficile. Mol. Microbiol. 71, 1308-1322 (2009).
    • (2009) Clostridium Difficile , pp. 1308-1322
    • Fagan, R.P.1
  • 9
    • 48149095082 scopus 로고    scopus 로고
    • The structure and binding behavior of the bacterial cell surface layer protein SbsC
    • Pavkov, T. etal. The structure and binding behavior of the bacterial cell surface layer protein SbsC. Structure 16, 1226-1237 (2008).
    • (2008) Structure , pp. 1226-1237
    • Pavkov, T.1
  • 10
    • 79960383869 scopus 로고    scopus 로고
    • Structure of surface layer homology (SLH) domains from Bacillus anthracis surface array protein
    • Kern, J. etal. Structure of surface layer homology (SLH) domains from Bacillus anthracis surface array protein. J. Biol. Chem. 286, 26042-26049 (2011).
    • (2011) J. Biol. Chem. , pp. 26042-26049
    • Kern, J.1
  • 11
    • 0032464347 scopus 로고    scopus 로고
    • Structural research on surface layers: A focus on stability, surface layer homology domains, and surface layer-cell wall interactions
    • Engelhardt, H. & Peters, J. Structural research on surface layers: a focus on stability, surface layer homology domains, and surface layer-cell wall interactions. J. Struct Biol. 124, 276-302 (1998).
    • (1998) J. Struct Biol. , pp. 276-302
    • Engelhardt, H.1    Peters, J.2
  • 12
    • 0036785598 scopus 로고    scopus 로고
    • Bindingof Clostridium difficile surface layer proteins to gastrointestinal tissues
    • Calabi, E., Calabi, F., Phillips, A. D.& Fairweather, N.F. Bindingof Clostridium difficile surface layer proteins to gastrointestinal tissues. Infect Immun. 70, 5770-5778 (2002).
    • (2002) Infect Immun , pp. 5770-5778
    • Calabi, E.1    Calabi, F.2    Phillips, A.D.3    Fairweather, N.F.4
  • 13
    • 74349118819 scopus 로고    scopus 로고
    • BslA, the S-layer adhesin of B. Anthracis
    • Kern, J. & Schneewind, O. BslA, the S-layer adhesin of B. anthracis, is a virulence factorforanthrax pathogenesis. Mol. Microbiol. 75, 324-332 (2010).
    • (2010) Mol. Microbiol. , pp. 324-332
    • Kern, J.1    Schneewind, O.2
  • 14
    • 80052083563 scopus 로고    scopus 로고
    • Nanobody stabilization of G protein-coupled receptor conformational states
    • Steyaert, J. & Kobilka, B. K. Nanobody stabilization of G protein-coupled receptor conformational states. Curr. Opin. Struct. Biol. 21, 567-572 (2011).
    • (2011) Curr. Opin. Struct. Biol. , pp. 567-572
    • Steyaert, J.1    Kobilka, B.K.2
  • 15
    • 0029876584 scopus 로고    scopus 로고
    • Dynamics in oxygen-induced changes in S-layer protein synthesis from BacillusstearothermophilusPV72 and the S-layer-deficient variant T5 in continuous culture and studies of the cell wall composition
    • Sara, M. etal. Dynamics in oxygen-induced changes in S-layer protein synthesis from Bacillusstearothermophilus PV72 and the S-layer-deficient variant T5 in continuous culture and studies of the cell wall composition. J. Bacteriol. 178, 2108-2117(1996).
    • (1996) J. Bacteriol. , pp. 2108-2117
    • Sara, M.1
  • 16
    • 1242339692 scopus 로고    scopus 로고
    • &Sara, M. Biophysical characterization of the entire bacterial surface layer protein SbsBand its two distinct functional domains
    • Runzler, D., Huber, C., Moll, D., Kohler, G. &Sara, M. Biophysical characterization of the entire bacterial surface layer protein SbsBand its two distinct functional domains. J. Biol. Chem. 279, 5207-5215 (2004).
    • (2004) J. Biol. Chem. , pp. 5207-5215
    • Runzler, D.1    Huber, C.2    Moll, D.3    Kohler, G.4
  • 17
    • 40049085132 scopus 로고    scopus 로고
    • The surface location of individual residues in a bacterial S-layer protein
    • Kinns, H. & Howorka, S. The surface location of individual residues in a bacterial S-layer protein. J. Mol. Biol. 377, 589-604 (2008).
    • (2008) J. Mol. Biol. , pp. 589-604
    • Kinns, H.1    Howorka, S.2
  • 19
    • 0037069325 scopus 로고    scopus 로고
    • S-layer-streptavidin fusion proteins as template for nanopatterned molecular arrays
    • Moll, D. etal. S-layer-streptavidin fusion proteins as template for nanopatterned molecular arrays. Proc. Nat Acad. Sci. USA 99, 14646-14651 (2002).
    • (2002) Proc. Nat Acad. Sci. USA , pp. 14646-14651
    • Moll, D.1
  • 20
    • 0345435047 scopus 로고    scopus 로고
    • Stabilizing effect of an S-layer on liposomes towards thermal or mechanical stress
    • Mader, C., Kupcu, S., Sara, M. & Sleytr, U. B. Stabilizing effect of an S-layer on liposomes towards thermal or mechanical stress. Biochim. Biophys.Acta 1418, 106-116(1999).
    • (1999) Biochim. Biophys.Acta , pp. 106-116
    • Mader, C.1    Kupcu, S.2    Sara, M.3    Sleytr, U.B.4
  • 21
    • 0032415871 scopus 로고    scopus 로고
    • Identification of two binding domains, one for peptidoglycan and another for a secondary cell wall polymer, on the N-terminal part of the S-layer protein SbsB from Bacillus stearothermophilus PV72/p2
    • Sara, M., Egelseer, E. M., Dekitsch, C. & Sleytr, U. B. Identification of two binding domains, one for peptidoglycan and another for a secondary cell wall polymer, on the N-terminal part of the S-layer protein SbsB from Bacillus stearothermophilus PV72/p2. J. Bacteriol. 180, 6780-6783 (1998).
    • (1998) J. Bacteriol. , pp. 6780-6783
    • Sara, M.1    Egelseer, E.M.2    Dekitsch, C.3    Sleytr, U.B.4
  • 23
    • 0037123593 scopus 로고    scopus 로고
    • C-cadherin ectodomain structure and implications for cell adhesion mechanisms
    • Boggon, T. J. etal. C-cadherin ectodomain structure and implications for cell adhesion mechanisms. Science 296, 1308-1313(2002).
    • (2002) Science , vol.296 , pp. 1308-1313
    • Boggon, T.J.1
  • 24
    • 45849137475 scopus 로고    scopus 로고
    • TheallostericroleoftheCa11 switch in adhesion and elasticity of C-cadherin
    • 11 switch in adhesion and elasticity of C-cadherin. Biophys.J. 94, 4621-4633 (2008).
    • (2008) Biophys.J. , pp. 4621-4633
    • Sotomayor, M.1    Schulten, K.2
  • 25
    • 0034528189 scopus 로고    scopus 로고
    • Surface-accessible residues in the monomeric and assembled forms of a bacterial surface layer protein
    • Howorka, S. etal. Surface-accessible residues in the monomeric and assembled forms of a bacterial surface layer protein. J. Biol. Chem. 275, 37876-37886 (2000).
    • (2000) J. Biol. Chem. , pp. 37876-37886
    • Howorka, S.1
  • 26
    • 78649891889 scopus 로고    scopus 로고
    • Structural changes of envelope proteins during alphavirus fusion
    • Li, L., Jose, J., Xiang, Y., Kuhn, R. J. & Rossmann, M. G. Structural changes of envelope proteins during alphavirus fusion. Nature 468, 705-708 (2010).
    • (2010) Nature , pp. 705-708
    • Li, L.1    Jose, J.2    Xiang, Y.3    Kuhn, R.J.4    Rossmann, M.G.5
  • 27
    • 78649817910 scopus 로고    scopus 로고
    • Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography
    • Voss, J. E. etal. Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography. Nature 468, 709-712 (2010).
    • (2010) Nature , pp. 709-712
    • Voss, J.E.1
  • 28
  • 29
    • 34848866243 scopus 로고    scopus 로고
    • Structure of full-length HIV-1CA: A model forthe mature capsid lattice
    • Ganser-Pornillos, B. K., Cheng, A. & Yeager, M. Structure of full-length HIV-1CA: a model forthe mature capsid lattice. Cell 131, 70-79 (2007).
    • (2007) Cell , pp. 70-79
    • Ganser-Pornillos, B.K.1    Cheng, A.2    Yeager, M.3
  • 30
    • 11144241270 scopus 로고    scopus 로고
    • Chemical basis for the affinity maturation of a camel single domain antibody
    • De Genst, E. etal. Chemical basis for the affinity maturation of a camel single domain antibody. J. Biol. Chem. 279, 53593-53601 (2004).
    • (2004) J. Biol. Chem. , pp. 53593-53601
    • De Genst, E.1
  • 32
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and post-refinement
    • Kabsch, W. Integration, scaling, space-group assignment and post-refinement. Acta Crystallogr. D Biol. Crystallogr. 66, 133-144 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , pp. 133-144
    • Kabsch, W.1
  • 33
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P.D. etal. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol Crystallogr. , pp. 213-221
    • Adams, P.D.1
  • 35
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov, G. N. etal. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D Biol. Crystallogr. 67, 355-367 (2011).
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , pp. 355-367
    • Murshudov, G.N.1
  • 36
    • 0141484613 scopus 로고    scopus 로고
    • &Svergun, D. I. PRIMUS: A Windows PC-based system for small-angle scattering data analysis
    • Konarev, P., Volkov, V.V., Sokolova, A. V., Koch, M. H. J. &Svergun, D. I. PRIMUS: a Windows PC-based system for small-angle scattering data analysis. J.Apl. Cryst 36, 1277-1282 (2003).
    • (2003) J.Apl. Cryst , pp. 1277-1282
    • Konarev, P.1    Volkov, V.V.2    Sokolova, A.V.3    Koch, M.H.J.4
  • 37
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Cryst. 25, 495-503 (1992).
    • (1992) J. Appl. Cryst. , pp. 495-503
    • Svergun, D.I.1
  • 38
    • 0029185933 scopus 로고
    • CRYSOL—a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D. I., Barberato, C. & Koch, M. H. J. CRYSOL—a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J.Appl. Cryst 28, 768-773 (1995).
    • (1995) J.Appl. Cryst , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 39
    • 0035010533 scopus 로고    scopus 로고
    • &Koch, M. H. Determination of domain structure of proteins from X-ray solution scattering
    • Svergun, D. I., Petoukhov, M. V. &Koch, M. H. Determination of domain structure of proteins from X-ray solution scattering. Biophys.J. 80, 2946-2953 (2001).
    • (2001) Biophys.J. , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2
  • 40
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin, M. B. & Svergun, D. I. Automated matching of high- and low-resolution structural models. J. Appl. Cryst 34, 33-41 (2001).
    • (2001) J. Appl. Cryst , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 41
    • 77955358961 scopus 로고    scopus 로고
    • Using Situs for the integration of multi-resolution structures
    • Wriggers, W. Using Situs for the integration of multi-resolution structures. Biophys. Rev. 2, 21-27(2010).
    • (2010) Biophys. Rev. , pp. 21-27
    • Wriggers, W.1
  • 42
    • 4444221565 scopus 로고    scopus 로고
    • F. Etal.UCSF Chimera—a visualization system for exploratory research and analysis
    • Pettersen, E. F. etal. UCSF Chimera—a visualization system for exploratory research and analysis. J. Comput Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput Chem. , pp. 1605-1612
    • Pettersen, E.1
  • 44
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell, J. A. & Grigorieff, N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct Biol. 142, 334-347 (2003).
    • (2003) J. Struct Biol. , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 45
    • 36049000626 scopus 로고    scopus 로고
    • 2dx_merge: Data management and merging for 2D crystal images
    • Gipson, B., Zeng, X.& Stahlberg, H.2dx_merge: data management and merging for 2D crystal images. J. Struct Biol. 160, 375-384 (2007).
    • (2007) J. Struct Biol. , pp. 375-384
    • Gipson, B.1    Zeng, X.2    Stahlberg, H.3
  • 46
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Number 4
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crysta//ogr. D Bio/. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crysta//Ogr. D Bio/. Crystallogr. , pp. 760-763
  • 47
    • 0242663237 scopus 로고    scopus 로고
    • A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations
    • Duan, Y. etal. A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations. J. Comput. Chem. 24, 1999-2012 (2003).
    • (2003) J. Comput. Chem. , pp. 1999-2012
    • Duan, Y.1


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