메뉴 건너뛰기




Volumn 364, Issue 4, 2006, Pages 716-734

In Meso Structure of the Cobalamin Transporter, BtuB, at 1.95 Å Resolution

Author keywords

colicin; cubic phase; membrane protein crystals; vitamin B12; X ray diffraction

Indexed keywords

BETA FACTOR; CARRIER PROTEIN; COBALAMIN TRANSPORTER; LIPID; MEMBRANE PROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 33750965918     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.09.022     Document Type: Article
Times cited : (89)

References (41)
  • 1
    • 0032553533 scopus 로고    scopus 로고
    • Purification and characterization of monomeric Escherichia coli vitamin B12 receptor with high affinity for colicin E3
    • Taylor R., Burgner J.W., Clifton J., and Cramer W.A. Purification and characterization of monomeric Escherichia coli vitamin B12 receptor with high affinity for colicin E3. J. Biol. Chem. 273 (1998) 31113-31118
    • (1998) J. Biol. Chem. , vol.273 , pp. 31113-31118
    • Taylor, R.1    Burgner, J.W.2    Clifton, J.3    Cramer, W.A.4
  • 2
    • 0036589166 scopus 로고    scopus 로고
    • The Tol proteins of Escherichia coli and their involvement in the translocation of group A colicins
    • Lazzaroni J.C., Dubuisson J.F., and Vianney A. The Tol proteins of Escherichia coli and their involvement in the translocation of group A colicins. Biochimie 84 (2002) 391-397
    • (2002) Biochimie , vol.84 , pp. 391-397
    • Lazzaroni, J.C.1    Dubuisson, J.F.2    Vianney, A.3
  • 3
    • 0242670022 scopus 로고    scopus 로고
    • Substrate-induced transmembrane signaling in the cobalamin transporter BtuB
    • Chimento D.P., Mohanty A.K., Kadner R.J., and Wiener M.C. Substrate-induced transmembrane signaling in the cobalamin transporter BtuB. Nature Struct. Biol. 10 (2003) 394-401
    • (2003) Nature Struct. Biol. , vol.10 , pp. 394-401
    • Chimento, D.P.1    Mohanty, A.K.2    Kadner, R.J.3    Wiener, M.C.4
  • 4
    • 0242569215 scopus 로고    scopus 로고
    • Spectroscopic evidence that osmolytes used in crystallization buffers inhibit a conformation change in a membrane protein
    • Fanucci G.E., Lee J.Y., and Cafiso D.S. Spectroscopic evidence that osmolytes used in crystallization buffers inhibit a conformation change in a membrane protein. Biochemistry 42 (2003) 13106-13112
    • (2003) Biochemistry , vol.42 , pp. 13106-13112
    • Fanucci, G.E.1    Lee, J.Y.2    Cafiso, D.S.3
  • 5
    • 0037452539 scopus 로고    scopus 로고
    • Substrate-induced conformational changes of the periplasmic N-terminus of an outer-membrane transporter by site-directed spin labeling
    • Fanucci G.E., Coggshall K.A., Cadieux N., Kim M., Kadner R.J., and Cafiso D.S. Substrate-induced conformational changes of the periplasmic N-terminus of an outer-membrane transporter by site-directed spin labeling. Biochemistry 42 (2003) 1391-1400
    • (2003) Biochemistry , vol.42 , pp. 1391-1400
    • Fanucci, G.E.1    Coggshall, K.A.2    Cadieux, N.3    Kim, M.4    Kadner, R.J.5    Cafiso, D.S.6
  • 6
    • 0141816803 scopus 로고    scopus 로고
    • Competing ligands stabilize alternate conformations of the energy coupling motif of a TonB-dependent outer membrane transporter
    • Fanucci G.E., Cadieux N., Kadner R.J., and Cafiso D.S. Competing ligands stabilize alternate conformations of the energy coupling motif of a TonB-dependent outer membrane transporter. Proc. Natl Acad. Sci. USA 100 (2003) 11382-11387
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 11382-11387
    • Fanucci, G.E.1    Cadieux, N.2    Kadner, R.J.3    Cafiso, D.S.4
  • 7
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: a novel concept for the crystallization of membrane proteins
    • Landau E.M., and Rosenbusch J.P. Lipidic cubic phases: a novel concept for the crystallization of membrane proteins. Proc. Natl Acad. Sci. USA 93 (1996) 14532-14535
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 8
    • 0037391107 scopus 로고    scopus 로고
    • Membrane protein crystallization
    • Caffrey M. Membrane protein crystallization. J. Struct. Biol. 142 (2003) 108-132
    • (2003) J. Struct. Biol. , vol.142 , pp. 108-132
    • Caffrey, M.1
  • 9
  • 10
    • 0242432342 scopus 로고    scopus 로고
    • Crystallization and initial X-ray diffraction of BtuB, the integral membrane cobalamin transporter of Escherichia coli
    • Chimento D.P., Mohanty A.K., Kadner R.J., and Wiener M.C. Crystallization and initial X-ray diffraction of BtuB, the integral membrane cobalamin transporter of Escherichia coli. Acta Crystallog. sect. D 59 (2003) 509-511
    • (2003) Acta Crystallog. sect. D , vol.59 , pp. 509-511
    • Chimento, D.P.1    Mohanty, A.K.2    Kadner, R.J.3    Wiener, M.C.4
  • 11
    • 33645054559 scopus 로고    scopus 로고
    • Room to move: crystallizing membrane proteins in swollen lipidic mesophases
    • Cherezov V., Clogston J., Papiz M.Z., and Caffrey M. Room to move: crystallizing membrane proteins in swollen lipidic mesophases. J. Mol. Biol. 357 (2006) 1605-1618
    • (2006) J. Mol. Biol. , vol.357 , pp. 1605-1618
    • Cherezov, V.1    Clogston, J.2    Papiz, M.Z.3    Caffrey, M.4
  • 12
    • 0242385349 scopus 로고    scopus 로고
    • Detergents destabilize the cubic phase of monoolein: implications for membrane protein crystallization
    • Misquitta Y., and Caffrey M. Detergents destabilize the cubic phase of monoolein: implications for membrane protein crystallization. Biophys. J. 85 (2003) 3084-3096
    • (2003) Biophys. J. , vol.85 , pp. 3084-3096
    • Misquitta, Y.1    Caffrey, M.2
  • 13
    • 15444380710 scopus 로고    scopus 로고
    • Gramicidin structure and disposition in highly curved membranes
    • Liu W., and Caffrey M. Gramicidin structure and disposition in highly curved membranes. J. Struct. Biol. 150 (2005) 23-40
    • (2005) J. Struct. Biol. , vol.150 , pp. 23-40
    • Liu, W.1    Caffrey, M.2
  • 14
    • 0023000315 scopus 로고
    • A requirement for calcium in the transport of cobalamin across the outer membrane of Escherichia coli
    • Bradbeer C., Reynolds P.R., Bauler G.M., and Fernandez M.T. A requirement for calcium in the transport of cobalamin across the outer membrane of Escherichia coli. J. Biol. Chem. 261 (1986) 2520-2523
    • (1986) J. Biol. Chem. , vol.261 , pp. 2520-2523
    • Bradbeer, C.1    Reynolds, P.R.2    Bauler, G.M.3    Fernandez, M.T.4
  • 17
    • 33744780736 scopus 로고    scopus 로고
    • Outer membrane active transport: structure of the BtuB:TonB complex
    • Shultis D.D., Purdy M.D., Banchs C.N., and Wiener M.C. Outer membrane active transport: structure of the BtuB:TonB complex. Science 312 (2006) 1396-1399
    • (2006) Science , vol.312 , pp. 1396-1399
    • Shultis, D.D.1    Purdy, M.D.2    Banchs, C.N.3    Wiener, M.C.4
  • 19
    • 0030148764 scopus 로고    scopus 로고
    • The temperature-composition phase diagram and mesophase structure characterization of the monoolein/water system
    • Briggs J., Chung H., and Caffrey M. The temperature-composition phase diagram and mesophase structure characterization of the monoolein/water system. J. Phys. II France 6 (1996) 723-751
    • (1996) J. Phys. II France , vol.6 , pp. 723-751
    • Briggs, J.1    Chung, H.2    Caffrey, M.3
  • 20
    • 0034717007 scopus 로고    scopus 로고
    • Structure of the light-driven chloride pump halorhodopsin at 1.8 Å resolution
    • Kolbe M., Besir H., Essen L.O., and Oesterhelt D. Structure of the light-driven chloride pump halorhodopsin at 1.8 Å resolution. Science 288 (2000) 1390-1396
    • (2000) Science , vol.288 , pp. 1390-1396
    • Kolbe, M.1    Besir, H.2    Essen, L.O.3    Oesterhelt, D.4
  • 21
    • 1842502604 scopus 로고    scopus 로고
    • X-Ray structure determination of three mutants of the bacterial photosynthetic reaction centers from Rb. sphaeroides; altered proton transfer pathways
    • Xu Q., Axelrod H.L., Abresch E.C., Paddock M.L., Okamura M.Y., and Feher G. X-Ray structure determination of three mutants of the bacterial photosynthetic reaction centers from Rb. sphaeroides; altered proton transfer pathways. Structure 12 (2004) 703-715
    • (2004) Structure , vol.12 , pp. 703-715
    • Xu, Q.1    Axelrod, H.L.2    Abresch, E.C.3    Paddock, M.L.4    Okamura, M.Y.5    Feher, G.6
  • 22
    • 0038724257 scopus 로고    scopus 로고
    • Membrane protein dynamics versus environment: simulations of OmpA in a micelle and in a bilayer
    • Bond P.J., and Sansom M.S. Membrane protein dynamics versus environment: simulations of OmpA in a micelle and in a bilayer. J. Mol. Biol. 329 (2003) 1035-1053
    • (2003) J. Mol. Biol. , vol.329 , pp. 1035-1053
    • Bond, P.J.1    Sansom, M.S.2
  • 24
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • McHaourab H.S., Lietzow M.A., Hideg K., and Hubbell W.L. Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics. Biochemistry 35 (1996) 7692-7704
    • (1996) Biochemistry , vol.35 , pp. 7692-7704
    • McHaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 26
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: physical principles
    • White S.H., and Wimley W.C. Membrane protein folding and stability: physical principles. Annu. Rev. Biophys. Biomol. Struct. 28 (1999) 319-365
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 28
    • 0032422462 scopus 로고    scopus 로고
    • A simple mechanical mixer for small viscous lipid-containing samples
    • Cheng A., Hummel B., Qiu H., and Caffrey M. A simple mechanical mixer for small viscous lipid-containing samples. Chem. Phys. Lipids. 95 (1998) 11-21
    • (1998) Chem. Phys. Lipids. , vol.95 , pp. 11-21
    • Cheng, A.1    Hummel, B.2    Qiu, H.3    Caffrey, M.4
  • 29
    • 11744300646 scopus 로고    scopus 로고
    • Lyotropic and thermotropic phase behavior of hydrated monoacylglycerols: structure characterization of monovaccenin
    • Qiu H., and Caffrey M. Lyotropic and thermotropic phase behavior of hydrated monoacylglycerols: structure characterization of monovaccenin. J. Phys. Chem. B 102 (1998) 4819-4829
    • (1998) J. Phys. Chem. B , vol.102 , pp. 4819-4829
    • Qiu, H.1    Caffrey, M.2
  • 31
    • 84971942068 scopus 로고
    • JCPDS-International Centre for diffraction data round robin study of silver behenate. A possible low-angle X-ray diffraction calibration standard
    • Blanton T.N., Huang T.C., Toraya H., Hubbard C.R., Robie S.B., Louer D., et al. JCPDS-International Centre for diffraction data round robin study of silver behenate. A possible low-angle X-ray diffraction calibration standard. Powder Diffr. 10 (1995) 91-95
    • (1995) Powder Diffr. , vol.10 , pp. 91-95
    • Blanton, T.N.1    Huang, T.C.2    Toraya, H.3    Hubbard, C.R.4    Robie, S.B.5    Louer, D.6
  • 32
    • 0028070558 scopus 로고
    • The temperature-composition phase diagram and mesophase structure characterization of monopentadecenoin in water
    • Briggs J., and Caffrey M. The temperature-composition phase diagram and mesophase structure characterization of monopentadecenoin in water. Biophys. J. 67 (1994) 1594-1602
    • (1994) Biophys. J. , vol.67 , pp. 1594-1602
    • Briggs, J.1    Caffrey, M.2
  • 33
    • 0034901552 scopus 로고    scopus 로고
    • Rational design of lipid molecular structure: a case study involving the C19:1c10 monoacylglycerol
    • Misquitta Y., and Caffrey M. Rational design of lipid molecular structure: a case study involving the C19:1c10 monoacylglycerol. Biophys. J. 81 (2001) 1047-1058
    • (2001) Biophys. J. , vol.81 , pp. 1047-1058
    • Misquitta, Y.1    Caffrey, M.2
  • 34
    • 24344439854 scopus 로고    scopus 로고
    • Controlling release from the lipidic cubic phase. Amino acids, peptides, proteins and nucleic acids
    • Clogston J., and Caffrey M. Controlling release from the lipidic cubic phase. Amino acids, peptides, proteins and nucleic acids. J. Control Release 107 (2005) 97-111
    • (2005) J. Control Release , vol.107 , pp. 97-111
    • Clogston, J.1    Caffrey, M.2
  • 35
    • 37049058055 scopus 로고
    • The chemistry of vitamin B12. Part I. The valency and spectrum of the coenzyme
    • Hill J.A., Pratt J.M., and Williams R.J.P. The chemistry of vitamin B12. Part I. The valency and spectrum of the coenzyme. J. Chem. Soc. (London) (1964) 5149-5153
    • (1964) J. Chem. Soc. (London) , pp. 5149-5153
    • Hill, J.A.1    Pratt, J.M.2    Williams, R.J.P.3
  • 37
    • 0242367561 scopus 로고    scopus 로고
    • Nano-volume plates with excellent optical properties for fast, inexpensive crystallization screening of membrane proteins
    • Cherezov V., and Caffrey M. Nano-volume plates with excellent optical properties for fast, inexpensive crystallization screening of membrane proteins. J. Appl. Crystallog. 36 (2003) 1372-1377
    • (2003) J. Appl. Crystallog. , vol.36 , pp. 1372-1377
    • Cherezov, V.1    Caffrey, M.2
  • 38
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 39
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
  • 40
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 41
    • 16344373729 scopus 로고    scopus 로고
    • Comparative structural analysis of TonB-dependent outer membrane transporters: implications for the transport cycle
    • Chimento D.P., Kadner R.J., and Wiener M.C. Comparative structural analysis of TonB-dependent outer membrane transporters: implications for the transport cycle. Proteins: Struct. Funct. Genet. 59 (2005) 240-251
    • (2005) Proteins: Struct. Funct. Genet. , vol.59 , pp. 240-251
    • Chimento, D.P.1    Kadner, R.J.2    Wiener, M.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.