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Volumn 102, Issue 4, 2012, Pages 916-926

A delicate interplay of structure, dynamics, and thermodynamics for function: A high pressure NMR study of outer surface protein A

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL VACCINE; LIPOPROTEIN; MEMBRANE ANTIGEN; OUTER MEMBRANE PROTEIN; OUTER SURFACE PROTEIN A;

EID: 84857311961     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.12.010     Document Type: Article
Times cited : (28)

References (44)
  • 1
    • 0034912667 scopus 로고    scopus 로고
    • On-line cell high-pressure nuclear magnetic resonance technique: Application to protein studies
    • K. Akasaka, and H. Yamada On-line cell high-pressure nuclear magnetic resonance technique: application to protein studies Methods Enzymol. 338 2001 134 158
    • (2001) Methods Enzymol. , vol.338 , pp. 134-158
    • Akasaka, K.1    Yamada, H.2
  • 2
    • 33646900712 scopus 로고    scopus 로고
    • Probing conformational fluctuation of proteins by pressure perturbation
    • K. Akasaka Probing conformational fluctuation of proteins by pressure perturbation Chem. Rev. 106 2006 1814 1835
    • (2006) Chem. Rev. , vol.106 , pp. 1814-1835
    • Akasaka, K.1
  • 3
    • 0037452877 scopus 로고    scopus 로고
    • Close identity of a pressure-stabilized intermediate with a kinetic intermediate in protein folding
    • R. Kitahara, and K. Akasaka Close identity of a pressure-stabilized intermediate with a kinetic intermediate in protein folding Proc. Natl. Acad. Sci. USA 100 2003 3167 3172
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3167-3172
    • Kitahara, R.1    Akasaka, K.2
  • 4
    • 0034711091 scopus 로고    scopus 로고
    • High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase
    • R. Kitahara, and S. Sareth K. Akasaka High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase Biochemistry 39 2000 12789 12795
    • (2000) Biochemistry , vol.39 , pp. 12789-12795
    • Kitahara, R.1    Sareth, S.2    Akasaka, K.3
  • 5
    • 14644424521 scopus 로고    scopus 로고
    • NMR snapshots of a fluctuating protein structure: Ubiquitin at 30 bar-3 kbar
    • R. Kitahara, S. Yokoyama, and K. Akasaka NMR snapshots of a fluctuating protein structure: ubiquitin at 30 bar-3 kbar J. Mol. Biol. 347 2005 277 285
    • (2005) J. Mol. Biol. , vol.347 , pp. 277-285
    • Kitahara, R.1    Yokoyama, S.2    Akasaka, K.3
  • 6
    • 33748935136 scopus 로고    scopus 로고
    • Evolutionally conserved intermediates between ubiquitin and NEDD8
    • R. Kitahara, and Y. Yamaguchi K. Akasaka Evolutionally conserved intermediates between ubiquitin and NEDD8 J. Mol. Biol. 363 2006 395 404
    • (2006) J. Mol. Biol. , vol.363 , pp. 395-404
    • Kitahara, R.1    Yamaguchi, Y.2    Akasaka, K.3
  • 7
    • 70349606921 scopus 로고    scopus 로고
    • Pressure-dependent structure changes in barnase on ligand binding reveal intermediate rate fluctuations
    • D.J. Wilton, and R. Kitahara M.P. Williamson Pressure-dependent structure changes in barnase on ligand binding reveal intermediate rate fluctuations Biophys. J. 97 2009 1482 1490
    • (2009) Biophys. J. , vol.97 , pp. 1482-1490
    • Wilton, D.J.1    Kitahara, R.2    Williamson, M.P.3
  • 8
    • 0030932886 scopus 로고    scopus 로고
    • Crystal structure of Lyme disease antigen outer surface protein A complexed with an Fab
    • H. Li, and J.J. Dunn C.L. Lawson Crystal structure of Lyme disease antigen outer surface protein A complexed with an Fab Proc. Natl. Acad. Sci. USA 94 1997 3584 3589
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3584-3589
    • Li, H.1    Dunn, J.J.2    Lawson, C.L.3
  • 9
    • 33746565309 scopus 로고    scopus 로고
    • Atomic-resolution crystal structure of Borrelia burgdorferi outer surface protein A via surface engineering
    • K. Makabe, and V. Tereshko S. Koide Atomic-resolution crystal structure of Borrelia burgdorferi outer surface protein A via surface engineering Protein Sci. 15 2006 1907 1914
    • (2006) Protein Sci. , vol.15 , pp. 1907-1914
    • Makabe, K.1    Tereshko, V.2    Koide, S.3
  • 10
    • 0031913174 scopus 로고    scopus 로고
    • Studies on OspA: A source of new paradigms in Lyme disease research
    • M.T. Philipp Studies on OspA: a source of new paradigms in Lyme disease research Trends Microbiol. 6 1998 44 47
    • (1998) Trends Microbiol. , vol.6 , pp. 44-47
    • Philipp, M.T.1
  • 11
    • 0033863073 scopus 로고    scopus 로고
    • Attachment of Borrelia burgdorferi within Ixodes scapularis mediated by outer surface protein A
    • U. Pal, and A.M. de Silva E. Fikrig Attachment of Borrelia burgdorferi within Ixodes scapularis mediated by outer surface protein A J. Clin. Invest. 106 2000 561 569
    • (2000) J. Clin. Invest. , vol.106 , pp. 561-569
    • Pal, U.1    De Silva, A.M.2    Fikrig, E.3
  • 12
    • 8344262276 scopus 로고    scopus 로고
    • TROSPA, an Ixodes scapularis receptor for Borrelia burgdorferi
    • U. Pal, and X. Li E. Fikrig TROSPA, an Ixodes scapularis receptor for Borrelia burgdorferi Cell 119 2004 457 468
    • (2004) Cell , vol.119 , pp. 457-468
    • Pal, U.1    Li, X.2    Fikrig, E.3
  • 13
    • 20444415308 scopus 로고    scopus 로고
    • Structure-based design of a second-generation Lyme disease vaccine based on a C-terminal fragment of Borrelia burgdorferi OspA
    • S. Koide, and X. Yang B.J. Luft Structure-based design of a second-generation Lyme disease vaccine based on a C-terminal fragment of Borrelia burgdorferi OspA J. Mol. Biol. 350 2005 290 299
    • (2005) J. Mol. Biol. , vol.350 , pp. 290-299
    • Koide, S.1    Yang, X.2    Luft, B.J.3
  • 14
    • 0034613035 scopus 로고    scopus 로고
    • Structural identification of a key protective B-cell epitope in Lyme disease antigen OspA
    • W. Ding, and X. Huang C.L. Lawson Structural identification of a key protective B-cell epitope in Lyme disease antigen OspA J. Mol. Biol. 302 2000 1153 1164
    • (2000) J. Mol. Biol. , vol.302 , pp. 1153-1164
    • Ding, W.1    Huang, X.2    Lawson, C.L.3
  • 15
    • 0031885491 scopus 로고    scopus 로고
    • A stable single-layer β-sheet without a hydrophobic core
    • T.N. Pham, A. Koide, and S. Koide A stable single-layer β-sheet without a hydrophobic core Nat. Struct. Biol. 5 1998 115 119
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 115-119
    • Pham, T.N.1    Koide, A.2    Koide, S.3
  • 16
    • 33947314274 scopus 로고    scopus 로고
    • Hydrophobic surface burial is the major stability determinant of a flat, single-layer β-sheet
    • S. Yan, and G. Gawlak S. Koide Hydrophobic surface burial is the major stability determinant of a flat, single-layer β-sheet J. Mol. Biol. 368 2007 230 243
    • (2007) J. Mol. Biol. , vol.368 , pp. 230-243
    • Yan, S.1    Gawlak, G.2    Koide, S.3
  • 17
    • 0036408312 scopus 로고    scopus 로고
    • Thermodynamic and kinetic exploration of the energy landscape of Borrelia burgdorferi OspA by native-state hydrogen exchange
    • S. Yan, S.D. Kennedy, and S. Koide Thermodynamic and kinetic exploration of the energy landscape of Borrelia burgdorferi OspA by native-state hydrogen exchange J. Mol. Biol. 323 2002 363 375
    • (2002) J. Mol. Biol. , vol.323 , pp. 363-375
    • Yan, S.1    Kennedy, S.D.2    Koide, S.3
  • 18
    • 0037073474 scopus 로고    scopus 로고
    • Backbone dynamics and thermodynamics of Borrelia outer surface protein A
    • N.H. Pawley, S. Koide, and L.K. Nicholson Backbone dynamics and thermodynamics of Borrelia outer surface protein A J. Mol. Biol. 324 2002 991 1002
    • (2002) J. Mol. Biol. , vol.324 , pp. 991-1002
    • Pawley, N.H.1    Koide, S.2    Nicholson, L.K.3
  • 19
    • 0036974249 scopus 로고    scopus 로고
    • Calorimetric dissection of thermal unfolding of OspA, a predominantly β-sheet protein containing a single-layer β-sheet
    • T. Nakagawa, and H. Shimizu A. Tamura Calorimetric dissection of thermal unfolding of OspA, a predominantly β-sheet protein containing a single-layer β-sheet J. Mol. Biol. 323 2002 751 762
    • (2002) J. Mol. Biol. , vol.323 , pp. 751-762
    • Nakagawa, T.1    Shimizu, H.2    Tamura, A.3
  • 20
    • 0142185486 scopus 로고    scopus 로고
    • Unfolding mechanics of multiple OspA substructures investigated with single molecule force spectroscopy
    • R. Hertadi, and F. Gruswitz A. Ikai Unfolding mechanics of multiple OspA substructures investigated with single molecule force spectroscopy J. Mol. Biol. 333 2003 993 1002
    • (2003) J. Mol. Biol. , vol.333 , pp. 993-1002
    • Hertadi, R.1    Gruswitz, F.2    Ikai, A.3
  • 21
    • 0033551095 scopus 로고    scopus 로고
    • Multistep denaturation of Borrelia burgdorferi OspA, a protein containing a single-layer β-sheet
    • S. Koide, and Z. Bu D.M. Engelman Multistep denaturation of Borrelia burgdorferi OspA, a protein containing a single-layer β-sheet Biochemistry 38 1999 4757 4767
    • (1999) Biochemistry , vol.38 , pp. 4757-4767
    • Koide, S.1    Bu, Z.2    Engelman, D.M.3
  • 22
    • 0032061808 scopus 로고    scopus 로고
    • NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer β-sheet
    • T.N. Pham, and S. Koide NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer β-sheet J. Biomol. NMR 11 1998 407 414
    • (1998) J. Biomol. NMR , vol.11 , pp. 407-414
    • Pham, T.N.1    Koide, S.2
  • 23
    • 0031674921 scopus 로고    scopus 로고
    • A solution SAXS study of Borrelia burgdorferi OspA, a protein containing a single-layer β-sheet
    • Z. Bu, S. Koide, and D.M. Engelman A solution SAXS study of Borrelia burgdorferi OspA, a protein containing a single-layer β-sheet Protein Sci. 7 1998 2681 2683
    • (1998) Protein Sci. , vol.7 , pp. 2681-2683
    • Bu, Z.1    Koide, S.2    Engelman, D.M.3
  • 24
    • 0032493678 scopus 로고    scopus 로고
    • NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies
    • X. Huang, and X. Yang S. Koide NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies J. Mol. Biol. 281 1998 61 67
    • (1998) J. Mol. Biol. , vol.281 , pp. 61-67
    • Huang, X.1    Yang, X.2    Koide, S.3
  • 25
    • 0035247443 scopus 로고    scopus 로고
    • Pressure-resisting cell for high-pressure, high-resolution nuclear magnetic resonance measurements at very high magnetic fields
    • H. Yamada, and K. Nishikawa K. Akasaka Pressure-resisting cell for high-pressure, high-resolution nuclear magnetic resonance measurements at very high magnetic fields Rev. Sci. Instrum. 72 2001 1463 1471
    • (2001) Rev. Sci. Instrum. , vol.72 , pp. 1463-1471
    • Yamada, H.1    Nishikawa, K.2    Akasaka, K.3
  • 26
    • 0030612833 scopus 로고    scopus 로고
    • 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution Proc. Natl. Acad. Sci. USA 94 1997 12366 12371
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wüthrich, K.3
  • 27
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • F. Delaglio, and S. Grzesiek A. Bax NMRPipe: a multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6 1995 277 293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Bax, A.3
  • 28
    • 34249765651 scopus 로고
    • NMR View: A computer program for the visualization and analysis of NMR data
    • B.A. Johnson, and R.A. Blevins NMR View: a computer program for the visualization and analysis of NMR data J. Biomol. NMR 4 1994 603 614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 29
    • 0000725483 scopus 로고
    • Thermodynamic fluctuations in protein molecules
    • A. Cooper Thermodynamic fluctuations in protein molecules Proc. Natl. Acad. Sci. USA 73 1976 2740 2741
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2740-2741
    • Cooper, A.1
  • 30
    • 0032477750 scopus 로고    scopus 로고
    • Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor
    • H. Li, H. Yamada, and K. Akasaka Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor Biochemistry 37 1998 1167 1173
    • (1998) Biochemistry , vol.37 , pp. 1167-1173
    • Li, H.1    Yamada, H.2    Akasaka, K.3
  • 31
    • 0042511922 scopus 로고    scopus 로고
    • The solution structure of bovine pancreatic trypsin inhibitor at high pressure
    • M.P. Williamson, K. Akasaka, and M. Refaee The solution structure of bovine pancreatic trypsin inhibitor at high pressure Protein Sci. 12 2003 1971 1979
    • (2003) Protein Sci. , vol.12 , pp. 1971-1979
    • Williamson, M.P.1    Akasaka, K.2    Refaee, M.3
  • 35
    • 0037171140 scopus 로고    scopus 로고
    • Revisiting volume changes in pressure-induced protein unfolding
    • C.A. Royer Revisiting volume changes in pressure-induced protein unfolding Biochim. Biophys. Acta 1595 2002 201 209
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 201-209
    • Royer, C.A.1
  • 36
    • 0344603844 scopus 로고    scopus 로고
    • The hydrogen exchange core and protein folding
    • R. Li, and C. Woodward The hydrogen exchange core and protein folding Protein Sci. 8 1999 1571 1590
    • (1999) Protein Sci. , vol.8 , pp. 1571-1590
    • Li, R.1    Woodward, C.2
  • 37
    • 0037214137 scopus 로고    scopus 로고
    • Protein hydrogen exchange mechanism: Local fluctuations
    • H. Maity, and W.K. Lim S.W. Englander Protein hydrogen exchange mechanism: local fluctuations Protein Sci. 12 2003 153 160
    • (2003) Protein Sci. , vol.12 , pp. 153-160
    • Maity, H.1    Lim, W.K.2    Englander, S.W.3
  • 38
    • 0017859780 scopus 로고
    • Unusual segmental flexibility in a region of tobacco mosaic virus coat protein
    • O. Jardetzky, and K. Akasaka K.C. Holmes Unusual segmental flexibility in a region of tobacco mosaic virus coat protein Nature 273 1978 564 566
    • (1978) Nature , vol.273 , pp. 564-566
    • Jardetzky, O.1    Akasaka, K.2    Holmes, K.C.3
  • 39
    • 2242483035 scopus 로고
    • Functional significance of flexibility in proteins
    • R. Huber, and W.S. Bennett Jr. Functional significance of flexibility in proteins Pure Appl. Chem. 54 1982 2489 2500
    • (1982) Pure Appl. Chem. , vol.54 , pp. 2489-2500
    • Huber, R.1    Bennett, Jr.W.S.2
  • 40
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat. Rev. Mol. Cell Biol. 6 2005 197 208
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 41
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • 29-32
    • R. Koradi, M. Billeter, and K. Wüthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55 29-32
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 42
    • 27744467601 scopus 로고
    • Activation and reaction volumes in solution
    • T. Asano, and W.J. le Noble Activation and reaction volumes in solution Chem. Rev. 78 1978 407 489
    • (1978) Chem. Rev. , vol.78 , pp. 407-489
    • Asano, T.1    Le Noble, W.J.2
  • 43
    • 0029963645 scopus 로고    scopus 로고
    • High-resolution triple-resonance NMR spectroscopy of a novel calmodulin-peptide complex at kilobar pressures
    • J.L. Urbauer, and M.R. Ehrhardt A.J. Wand High-resolution triple-resonance NMR spectroscopy of a novel calmodulin-peptide complex at kilobar pressures J. Am. Chem. Soc. 118 1996 11329 11330
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11329-11330
    • Urbauer, J.L.1    Ehrhardt, M.R.2    Wand, A.J.3
  • 44
    • 79955975933 scopus 로고    scopus 로고
    • Cavity hydration as a gateway to unfolding: An NMR study of hen lysozyme at high pressure and low temperature
    • Y.O. Kamatari, and L.J. Smith K. Akasaka Cavity hydration as a gateway to unfolding: an NMR study of hen lysozyme at high pressure and low temperature Biophys. Chem. 156 2011 24 30
    • (2011) Biophys. Chem. , vol.156 , pp. 24-30
    • Kamatari, Y.O.1    Smith, L.J.2    Akasaka, K.3


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