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Volumn 22, Issue 5, 2014, Pages 781-790

Mass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA

Author keywords

[No Author keywords available]

Indexed keywords

MULTIDRUG RESISTANCE PROTEIN; OUTER MEMBRANE PROTEIN A; MICELLE; OMPA OUTER MEMBRANE PROTEINS; OUTER MEMBRANE PROTEIN;

EID: 84899817875     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.03.004     Document Type: Article
Times cited : (52)

References (52)
  • 1
    • 0034695440 scopus 로고    scopus 로고
    • Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers
    • A. Arora, D. Rinehart, G. Szabo, and L.K. Tamm Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers J. Biol. Chem. 275 2000 1594 1600
    • (2000) J. Biol. Chem. , vol.275 , pp. 1594-1600
    • Arora, A.1    Rinehart, D.2    Szabo, G.3    Tamm, L.K.4
  • 2
    • 0035066331 scopus 로고    scopus 로고
    • Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
    • A. Arora, F. Abildgaard, J.H. Bushweller, and L.K. Tamm Structure of outer membrane protein A transmembrane domain by NMR spectroscopy Nat. Struct. Biol. 8 2001 334 338
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 334-338
    • Arora, A.1    Abildgaard, F.2    Bushweller, J.H.3    Tamm, L.K.4
  • 3
    • 82955168439 scopus 로고    scopus 로고
    • The polydispersity of αb-crystallin is rationalized by an interconverting polyhedral architecture
    • A.J. Baldwin, H. Lioe, G.R. Hilton, L.A. Baker, J.L. Rubinstein, L.E. Kay, and J.L. Benesch The polydispersity of αB-crystallin is rationalized by an interconverting polyhedral architecture Structure 19 2011 1855 1863
    • (2011) Structure , vol.19 , pp. 1855-1863
    • Baldwin, A.J.1    Lioe, H.2    Hilton, G.R.3    Baker, L.A.4    Rubinstein, J.L.5    Kay, L.E.6    Benesch, J.L.7
  • 5
    • 84871616988 scopus 로고    scopus 로고
    • The role of lipids in defining membrane protein interactions: Insights from mass spectrometry
    • N.P. Barrera, M. Zhou, and C.V. Robinson The role of lipids in defining membrane protein interactions: insights from mass spectrometry Trends Cell Biol. 23 2013 1 8
    • (2013) Trends Cell Biol. , vol.23 , pp. 1-8
    • Barrera, N.P.1    Zhou, M.2    Robinson, C.V.3
  • 6
    • 80053577815 scopus 로고    scopus 로고
    • Mass spectrometry: Come of age for structural and dynamical biology
    • J.L. Benesch, and B.T. Ruotolo Mass spectrometry: come of age for structural and dynamical biology Curr. Opin. Struct. Biol. 21 2011 641 649
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 641-649
    • Benesch, J.L.1    Ruotolo, B.T.2
  • 7
    • 0035996998 scopus 로고    scopus 로고
    • OmpA: A pore or not a pore? Simulation and modeling studies
    • P.J. Bond, J.D. Faraldo-Gómez, and M.S. Sansom OmpA: a pore or not a pore? Simulation and modeling studies Biophys. J. 83 2002 763 775
    • (2002) Biophys. J. , vol.83 , pp. 763-775
    • Bond, P.J.1    Faraldo-Gómez, J.D.2    Sansom, M.S.3
  • 8
    • 84876726004 scopus 로고    scopus 로고
    • Detergent release prolongs the lifetime of native-like membrane protein conformations in the gas-phase
    • A.J. Borysik, D.J. Hewitt, and C.V. Robinson Detergent release prolongs the lifetime of native-like membrane protein conformations in the gas-phase J. Am. Chem. Soc. 135 2013 6078 6083
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 6078-6083
    • Borysik, A.J.1    Hewitt, D.J.2    Robinson, C.V.3
  • 9
    • 78449267576 scopus 로고    scopus 로고
    • Collision cross sections of proteins and their complexes: A calibration framework and database for gas-phase structural biology
    • M.F. Bush, Z. Hall, K. Giles, J. Hoyes, C.V. Robinson, and B.T. Ruotolo Collision cross sections of proteins and their complexes: a calibration framework and database for gas-phase structural biology Anal. Chem. 82 2010 9557 9565
    • (2010) Anal. Chem. , vol.82 , pp. 9557-9565
    • Bush, M.F.1    Hall, Z.2    Giles, K.3    Hoyes, J.4    Robinson, C.V.5    Ruotolo, B.T.6
  • 10
    • 0028855096 scopus 로고
    • Naked protein conformations - Cytochrome-C in the gas-phase
    • D.E. Clemmer, R.R. Hudgins, and M.F. Jarrold Naked protein conformations - cytochrome-C in the gas-phase J. Am. Chem. Soc. 117 1995 10141 10142
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10141-10142
    • Clemmer, D.E.1    Hudgins, R.R.2    Jarrold, M.F.3
  • 11
    • 0028263998 scopus 로고
    • The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan
    • R. De Mot, and J. Vanderleyden The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan Mol. Microbiol. 12 1994 333 334
    • (1994) Mol. Microbiol. , vol.12 , pp. 333-334
    • De Mot, R.1    Vanderleyden, J.2
  • 12
    • 1442325407 scopus 로고    scopus 로고
    • Structure of the OmpA-like domain of RmpM from Neisseria meningitidis
    • S. Grizot, and S.K. Buchanan Structure of the OmpA-like domain of RmpM from Neisseria meningitidis Mol. Microbiol. 51 2004 1027 1037
    • (2004) Mol. Microbiol. , vol.51 , pp. 1027-1037
    • Grizot, S.1    Buchanan, S.K.2
  • 13
    • 84863416219 scopus 로고    scopus 로고
    • Charge-state dependent compaction and dissociation of protein complexes: Insights from ion mobility and molecular dynamics
    • Z. Hall, A. Politis, M.F. Bush, L.J. Smith, and C.V. Robinson Charge-state dependent compaction and dissociation of protein complexes: insights from ion mobility and molecular dynamics J. Am. Chem. Soc. 134 2012 3429 3438
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 3429-3438
    • Hall, Z.1    Politis, A.2    Bush, M.F.3    Smith, L.J.4    Robinson, C.V.5
  • 14
    • 84865788284 scopus 로고    scopus 로고
    • Structural modeling of heteromeric protein complexes from disassembly pathways and ion mobility-mass spectrometry
    • Z. Hall, A. Politis, and C.V. Robinson Structural modeling of heteromeric protein complexes from disassembly pathways and ion mobility-mass spectrometry Structure 20 2012 1596 1609
    • (2012) Structure , vol.20 , pp. 1596-1609
    • Hall, Z.1    Politis, A.2    Robinson, C.V.3
  • 15
    • 34347228701 scopus 로고    scopus 로고
    • Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry
    • H. Hernández, and C.V. Robinson Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry Nat. Protoc. 2 2007 715 726
    • (2007) Nat. Protoc. , vol.2 , pp. 715-726
    • Hernández, H.1    Robinson, C.V.2
  • 16
    • 33750255413 scopus 로고    scopus 로고
    • Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening
    • H. Hong, G. Szabo, and L.K. Tamm Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening Nat. Chem. Biol. 2 2006 627 635
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 627-635
    • Hong, H.1    Szabo, G.2    Tamm, L.K.3
  • 19
    • 84861451226 scopus 로고    scopus 로고
    • The bacterial outer membrane β-barrel assembly machinery
    • K.H. Kim, S. Aulakh, and M. Paetzel The bacterial outer membrane β-barrel assembly machinery Protein Sci. 21 2012 751 768
    • (2012) Protein Sci. , vol.21 , pp. 751-768
    • Kim, K.H.1    Aulakh, S.2    Paetzel, M.3
  • 20
    • 0033586795 scopus 로고    scopus 로고
    • Outer membrane protein A of Escherichia coli inserts and folds into lipid bilayers by a concerted mechanism
    • J.H. Kleinschmidt, T. den Blaauwen, A.J. Driessen, and L.K. Tamm Outer membrane protein A of Escherichia coli inserts and folds into lipid bilayers by a concerted mechanism Biochemistry 38 1999 5006 5016
    • (1999) Biochemistry , vol.38 , pp. 5006-5016
    • Kleinschmidt, J.H.1    Den Blaauwen, T.2    Driessen, A.J.3    Tamm, L.K.4
  • 21
    • 0348062818 scopus 로고    scopus 로고
    • The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models
    • J. Kopp, and T. Schwede The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models Nucleic Acids Res. 32 Database issue 2004 D230 D234
    • (2004) Nucleic Acids Res. , vol.32 , Issue.DATABASE ISSUE
    • Kopp, J.1    Schwede, T.2
  • 22
    • 84858445516 scopus 로고    scopus 로고
    • Outer membrane protein A and OprF: Versatile roles in Gram-negative bacterial infections
    • S. Krishnan, and N.V. Prasadarao Outer membrane protein A and OprF: versatile roles in Gram-negative bacterial infections FEBS J. 279 2012 919 931
    • (2012) FEBS J. , vol.279 , pp. 919-931
    • Krishnan, S.1    Prasadarao, N.V.2
  • 23
    • 0033601125 scopus 로고    scopus 로고
    • Structure and mechanism of yeast RNA triphosphatase: An essential component of the mRNA capping apparatus
    • C.D. Lima, L.K. Wang, and S. Shuman Structure and mechanism of yeast RNA triphosphatase: an essential component of the mRNA capping apparatus Cell 99 1999 533 543
    • (1999) Cell , vol.99 , pp. 533-543
    • Lima, C.D.1    Wang, L.K.2    Shuman, S.3
  • 24
    • 84883466602 scopus 로고    scopus 로고
    • Twenty years of gas phase structural biology
    • J. Marcoux, and C.V. Robinson Twenty years of gas phase structural biology Structure 21 2013 1541 1550
    • (2013) Structure , vol.21 , pp. 1541-1550
    • Marcoux, J.1    Robinson, C.V.2
  • 26
    • 84871981207 scopus 로고    scopus 로고
    • Intrinsically disordered p53 and its complexes populate compact conformations in the gas phase
    • K. Pagel, E. Natan, Z. Hall, A.R. Fersht, and C.V. Robinson Intrinsically disordered p53 and its complexes populate compact conformations in the gas phase Angew. Chem. Int. Ed. Engl. 52 2013 361 365
    • (2013) Angew. Chem. Int. Ed. Engl. , vol.52 , pp. 361-365
    • Pagel, K.1    Natan, E.2    Hall, Z.3    Fersht, A.R.4    Robinson, C.V.5
  • 27
  • 28
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • A. Pautsch, and G.E. Schulz Structure of the outer membrane protein A transmembrane domain Nat. Struct. Biol. 5 1998 1013 1017
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 29
    • 84887407837 scopus 로고    scopus 로고
    • Integrative modelling coupled with ion mobility mass spectrometry reveals structural features of the clamp loader in complex with single-stranded DNA binding protein
    • A. Politis, A.Y. Park, Z. Hall, B.T. Ruotolo, and C.V. Robinson Integrative modelling coupled with ion mobility mass spectrometry reveals structural features of the clamp loader in complex with single-stranded DNA binding protein J. Mol. Biol. 425 2013 4790 4801
    • (2013) J. Mol. Biol. , vol.425 , pp. 4790-4801
    • Politis, A.1    Park, A.Y.2    Hall, Z.3    Ruotolo, B.T.4    Robinson, C.V.5
  • 30
    • 84859498054 scopus 로고    scopus 로고
    • Outer membrane protein A (OmpA) of Shigella flexneri 2a links innate and adaptive immunity in a TLR2-dependent manner and involvement of IL-12 and nitric oxide
    • D. Pore, N. Mahata, and M.K. Chakrabarti Outer membrane protein A (OmpA) of Shigella flexneri 2a links innate and adaptive immunity in a TLR2-dependent manner and involvement of IL-12 and nitric oxide J. Biol. Chem. 287 2012 12589 12601
    • (2012) J. Biol. Chem. , vol.287 , pp. 12589-12601
    • Pore, D.1    Mahata, N.2    Chakrabarti, M.K.3
  • 31
    • 0036885109 scopus 로고    scopus 로고
    • A novel interaction of outer membrane protein A with C4b binding protein mediates serum resistance of Escherichia coli K1
    • N.V. Prasadarao, A.M. Blom, B.O. Villoutreix, and L.C. Linsangan A novel interaction of outer membrane protein A with C4b binding protein mediates serum resistance of Escherichia coli K1 J. Immunol. 169 2002 6352 6360
    • (2002) J. Immunol. , vol.169 , pp. 6352-6360
    • Prasadarao, N.V.1    Blom, A.M.2    Villoutreix, B.O.3    Linsangan, L.C.4
  • 37
    • 21644476468 scopus 로고    scopus 로고
    • PatchDock and SymmDock: Servers for rigid and symmetric docking
    • D. Schneidman-Duhovny, Y. Inbar, R. Nussinov, and H.J. Wolfson PatchDock and SymmDock: servers for rigid and symmetric docking Nucleic Acids Res. 33 Web Server issue 2005 W363 W367
    • (2005) Nucleic Acids Res. , vol.33 , Issue.WEB SERVER ISSUE
    • Schneidman-Duhovny, D.1    Inbar, Y.2    Nussinov, R.3    Wolfson, H.J.4
  • 40
    • 0035367725 scopus 로고    scopus 로고
    • Structural investigations of calcium binding and its role in activity and activation of outer membrane phospholipase A from Escherichia coli
    • H.J. Snijder, R.L. Kingma, K.H. Kalk, N. Dekker, M.R. Egmond, and B.W. Dijkstra Structural investigations of calcium binding and its role in activity and activation of outer membrane phospholipase A from Escherichia coli J. Mol. Biol. 309 2001 477 489
    • (2001) J. Mol. Biol. , vol.309 , pp. 477-489
    • Snijder, H.J.1    Kingma, R.L.2    Kalk, K.H.3    Dekker, N.4    Egmond, M.R.5    Dijkstra, B.W.6
  • 41
    • 0018150270 scopus 로고
    • Cell envelope and shape of Escherichia coli: Multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins
    • I. Sonntag, H. Schwarz, Y. Hirota, and U. Henning Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins J. Bacteriol. 136 1978 280 285
    • (1978) J. Bacteriol. , vol.136 , pp. 280-285
    • Sonntag, I.1    Schwarz, H.2    Hirota, Y.3    Henning, U.4
  • 44
    • 0026785288 scopus 로고
    • Pore-forming activity of OmpA protein of Escherichia coli
    • E. Sugawara, and H. Nikaido Pore-forming activity of OmpA protein of Escherichia coli J. Biol. Chem. 267 1992 2507 2511
    • (1992) J. Biol. Chem. , vol.267 , pp. 2507-2511
    • Sugawara, E.1    Nikaido, H.2
  • 45
    • 0028321391 scopus 로고
    • OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms
    • E. Sugawara, and H. Nikaido OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms J. Biol. Chem. 269 1994 17981 17987
    • (1994) J. Biol. Chem. , vol.269 , pp. 17981-17987
    • Sugawara, E.1    Nikaido, H.2
  • 46
    • 84866342585 scopus 로고    scopus 로고
    • OmpA is the principal nonspecific slow porin of Acinetobacter baumannii
    • E. Sugawara, and H. Nikaido OmpA is the principal nonspecific slow porin of Acinetobacter baumannii J. Bacteriol. 194 2012 4089 4096
    • (2012) J. Bacteriol. , vol.194 , pp. 4089-4096
    • Sugawara, E.1    Nikaido, H.2
  • 47
    • 33646339638 scopus 로고    scopus 로고
    • Outer membrane protein A of Escherichia coli O157:H7 stimulates dendritic cell activation
    • A.G. Torres, Y. Li, C.B. Tutt, L. Xin, T. Eaves-Pyles, and L. Soong Outer membrane protein A of Escherichia coli O157:H7 stimulates dendritic cell activation Infect. Immun. 74 2006 2676 2685
    • (2006) Infect. Immun. , vol.74 , pp. 2676-2685
    • Torres, A.G.1    Li, Y.2    Tutt, C.B.3    Xin, L.4    Eaves-Pyles, T.5    Soong, L.6
  • 48
    • 78649748259 scopus 로고    scopus 로고
    • Ion mobility mass spectrometry of two tetrameric membrane protein complexes reveals compact structures and differences in stability and packing
    • S.C. Wang, A. Politis, N. Di Bartolo, V.N. Bavro, S.J. Tucker, P.J. Booth, N.P. Barrera, and C.V. Robinson Ion mobility mass spectrometry of two tetrameric membrane protein complexes reveals compact structures and differences in stability and packing J. Am. Chem. Soc. 132 2010 15468 15470
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15468-15470
    • Wang, S.C.1    Politis, A.2    Di Bartolo, N.3    Bavro, V.N.4    Tucker, S.J.5    Booth, P.J.6    Barrera, N.P.7    Robinson, C.V.8
  • 49
    • 17844405030 scopus 로고    scopus 로고
    • Kinetics of folding of Escherichia coli OmpA from narrow to large pore conformation in a planar bilayer
    • E. Zakharian, and R.N. Reusch Kinetics of folding of Escherichia coli OmpA from narrow to large pore conformation in a planar bilayer Biochemistry 44 2005 6701 6707
    • (2005) Biochemistry , vol.44 , pp. 6701-6707
    • Zakharian, E.1    Reusch, R.N.2
  • 52
    • 84895079317 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry of a rotary ATPase reveals ATP-induced reduction in conformational flexibility
    • M. Zhou, A. Politis, R.B. Davies, I. Liko, K.J. Wu, A.G. Stewart, D. Stock, and C.V. Robinson Ion mobility-mass spectrometry of a rotary ATPase reveals ATP-induced reduction in conformational flexibility Nat. Chem. 6 2014 208 215
    • (2014) Nat. Chem. , vol.6 , pp. 208-215
    • Zhou, M.1    Politis, A.2    Davies, R.B.3    Liko, I.4    Wu, K.J.5    Stewart, A.G.6    Stock, D.7    Robinson, C.V.8


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