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Volumn 5, Issue , 2014, Pages

Mechanistic determinants of the directionality and energetics of active export by a heterodimeric ABC transporter

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ASPARTIC ACID; HETERODIMER; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; ANTIGEN; PROTEIN TRANSLOCASE; TRANSPORTER ASSOCIATED WITH ANTIGEN PROCESSING (TAP);

EID: 84921028041     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6419     Document Type: Article
Times cited : (82)

References (51)
  • 1
    • 4744358624 scopus 로고    scopus 로고
    • The ATP switch model for ABC transporters
    • Higgins, C. F. & Linton, K. J. The ATP switch model for ABC transporters. Nat. Struct. Mol. Biol. 11, 918-926 (2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 918-926
    • Higgins, C.F.1    Linton, K.J.2
  • 5
    • 4544336851 scopus 로고    scopus 로고
    • The ABCs of immunology: Structure and function of TAP, the transporter associated with antigen processing
    • Abele, R. & Tampé, R. The ABCs of immunology: structure and function of TAP, the transporter associated with antigen processing. Physiology 19, 216-224 (2004).
    • (2004) Physiology , vol.19 , pp. 216-224
    • Abele, R.1    Tampé, R.2
  • 6
    • 0036074018 scopus 로고    scopus 로고
    • Mammalian ABC transporters in health and disease
    • Borst, P. & Elferink, R. O. Mammalian ABC transporters in health and disease. Annu. Rev. Biochem. 71, 537-592 (2002).
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 537-592
    • Borst, P.1    Elferink, R.O.2
  • 7
    • 77955895736 scopus 로고    scopus 로고
    • ABC proteins in antigen translocation and viral inhibition
    • Parcej, D. & Tampé, R. ABC proteins in antigen translocation and viral inhibition. Nat. Chem. Biol. 6, 572-580 (2010).
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 572-580
    • Parcej, D.1    Tampé, R.2
  • 8
    • 70349333637 scopus 로고    scopus 로고
    • The mechanism of ABC transporters: General lessons from structural and functional studies of an antigenic peptide transporter
    • Procko, E., O'Mara, M. L., Bennett, W. F., Tieleman, D. P. & Gaudet, R. The mechanism of ABC transporters: general lessons from structural and functional studies of an antigenic peptide transporter. FASEB J. 23, 1287-1302 (2009).
    • (2009) FASEB J. , vol.23 , pp. 1287-1302
    • Procko, E.1    O'Mara, M.L.2    Bennett, W.F.3    Tieleman, D.P.4    Gaudet, R.5
  • 9
    • 84880756901 scopus 로고    scopus 로고
    • The MHC i loading complex: A multitasking machinery in adaptive immunity
    • Hulpke, S. & Tampé, R. The MHC I loading complex: a multitasking machinery in adaptive immunity. Trends Biochem. Sci. 38, 412-420 (2013).
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 412-420
    • Hulpke, S.1    Tampé, R.2
  • 10
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R. J. & Locher, K. P. Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185 (2006).
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 11
    • 63449139456 scopus 로고    scopus 로고
    • Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding
    • Aller, S. G. et al. Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding. Science 323, 1718-1722 (2009).
    • (2009) Science , vol.323 , pp. 1718-1722
    • Aller, S.G.1
  • 12
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • Ward, A., Reyes, C. L., Yu, J., Roth, C. B. & Chang, G. Flexibility in the ABC transporter MsbA: Alternating access with a twist. Proc. Natl Acad. Sci. USA 104, 19005-19010 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 13
    • 65249133460 scopus 로고    scopus 로고
    • Structural arrangement of the transmission interface in the antigen ABC transport complex TAP
    • Oancea, G. et al. Structural arrangement of the transmission interface in the antigen ABC transport complex TAP. Proc. Natl Acad. Sci. USA 106, 5551-5556 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 5551-5556
    • Oancea, G.1
  • 14
    • 8544269408 scopus 로고    scopus 로고
    • Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)
    • Chen, M., Abele, R. & Tampé, R. Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP). J. Biol. Chem. 279, 46073-46081 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 46073-46081
    • Chen, M.1    Abele, R.2    Tampé, R.3
  • 15
    • 0035912749 scopus 로고    scopus 로고
    • Use of chimeric proteins to investigate the role of transporter associated with antigen processing (TAP) structural domains in peptide binding and translocation
    • Arora, S., Lapinski, P. E. & Raghavan, M. Use of chimeric proteins to investigate the role of transporter associated with antigen processing (TAP) structural domains in peptide binding and translocation. Proc. Natl Acad. Sci. USA 98, 7241-7246 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 7241-7246
    • Arora, S.1    Lapinski, P.E.2    Raghavan, M.3
  • 16
    • 0035916358 scopus 로고    scopus 로고
    • Distinct functional properties of the TAP subunits coordinate the nucleotide-dependent transport cycle
    • Alberts, P., Daumke, O., Deverson, E. V., Howard, J. C. & Knittler, M. R. Distinct functional properties of the TAP subunits coordinate the nucleotide-dependent transport cycle. Curr. Biol. 11, 242-251 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 242-251
    • Alberts, P.1    Daumke, O.2    Deverson, E.V.3    Howard, J.C.4    Knittler, M.R.5
  • 17
    • 33749076230 scopus 로고    scopus 로고
    • Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter
    • Procko, E., Ferrin-O'Connell, I., Ng, S. L. & Gaudet, R. Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter. Mol. Cell 24, 51-62 (2006).
    • (2006) Mol. Cell , vol.24 , pp. 51-62
    • Procko, E.1    Ferrin-O'Connell, I.2    Ng, S.L.3    Gaudet, R.4
  • 18
    • 57649183334 scopus 로고    scopus 로고
    • Functional clustering of mutations in the dimer interface of the nucleotide binding folds of the sulfonylurea receptor
    • Masia, R. & Nichols, C. G. Functional clustering of mutations in the dimer interface of the nucleotide binding folds of the sulfonylurea receptor. J. Biol. Chem. 283, 30322-30329 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 30322-30329
    • Masia, R.1    Nichols, C.G.2
  • 19
    • 79953220143 scopus 로고    scopus 로고
    • Sequences in the nonconsensus nucleotide-binding domain of ABCG5/ABCG8 required for sterol transport
    • Wang, J. et al. Sequences in the nonconsensus nucleotide-binding domain of ABCG5/ABCG8 required for sterol transport. J. Biol. Chem. 286, 7308-7314 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 7308-7314
    • Wang, J.1
  • 20
    • 79953175250 scopus 로고    scopus 로고
    • Effects of the L511P and D512G mutations on the Escherichia coli ABC transporter MsbA
    • Schultz, K. M., Merten, J. A. & Klug, C. S. Effects of the L511P and D512G mutations on the Escherichia coli ABC transporter MsbA. Biochemistry 50, 2594-2602 (2011).
    • (2011) Biochemistry , vol.50 , pp. 2594-2602
    • Schultz, K.M.1    Merten, J.A.2    Klug, C.S.3
  • 21
    • 21244454073 scopus 로고    scopus 로고
    • H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
    • Zaitseva, J., Jenewein, S., Jumpertz, T., Holland, I. B. & Schmitt, L. H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB. EMBO J. 24, 1901-1910 (2005).
    • (2005) EMBO J. , vol.24 , pp. 1901-1910
    • Zaitseva, J.1    Jenewein, S.2    Jumpertz, T.3    Holland, I.B.4    Schmitt, L.5
  • 22
    • 79957932347 scopus 로고    scopus 로고
    • Crystal structure of the maltose transporter in a pretranslocation intermediate state
    • Oldham, M. L. & Chen, J. Crystal structure of the maltose transporter in a pretranslocation intermediate state. Science 332, 1202-1205 (2011).
    • (2011) Science , vol.332 , pp. 1202-1205
    • Oldham, M.L.1    Chen, J.2
  • 23
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith, P. C. et al. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10, 139-149 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 139-149
    • Smith, P.C.1
  • 24
    • 0033725154 scopus 로고    scopus 로고
    • Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel
    • Koopmann, J. O. et al. Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel. Immunity 13, 117-127 (2000).
    • (2000) Immunity , vol.13 , pp. 117-127
    • Koopmann, J.O.1
  • 25
    • 0037160075 scopus 로고    scopus 로고
    • A novel electron paramagnetic resonance approach to determine the mechanism of drug transport by P-glycoprotein
    • Omote, H. & Al-Shawi, M. K. A novel electron paramagnetic resonance approach to determine the mechanism of drug transport by P-glycoprotein. J. Biol. Chem. 277, 45688-45694 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 45688-45694
    • Omote, H.1    Al-Shawi, M.K.2
  • 26
    • 1642565130 scopus 로고    scopus 로고
    • Reversible transport by the ATP-binding cassette multidrug export pump LmrA: ATP synthesis at the expense of downhill ethidium uptake
    • Balakrishnan, L., Venter, H., Shilling, R. A. & van Veen, H. W. Reversible transport by the ATP-binding cassette multidrug export pump LmrA: ATP synthesis at the expense of downhill ethidium uptake. J. Biol. Chem. 279, 11273-11280 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 11273-11280
    • Balakrishnan, L.1    Venter, H.2    Shilling, R.A.3    Van Veen, H.W.4
  • 27
    • 0027239749 scopus 로고
    • Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter
    • Neefjes, J. J., Momburg, F. & Hämmerling, G. J. Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter. Science 261, 769-771 (1993).
    • (1993) Science , vol.261 , pp. 769-771
    • Neefjes, J.J.1    Momburg, F.2    Hämmerling, G.J.3
  • 28
    • 0043032667 scopus 로고    scopus 로고
    • Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing
    • Chen, M., Abele, R. & Tampé, R. Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing. J. Biol. Chem. 278, 29686-29692 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 29686-29692
    • Chen, M.1    Abele, R.2    Tampé, R.3
  • 29
    • 0037424544 scopus 로고    scopus 로고
    • Nucleotide interactions with membrane-bound transporter associated with antigen processing proteins
    • Lapinski, P. E., Raghuraman, G. & Raghavan, M. Nucleotide interactions with membrane-bound transporter associated with antigen processing proteins. J. Biol. Chem. 278, 8229-8237 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 8229-8237
    • Lapinski, P.E.1    Raghuraman, G.2    Raghavan, M.3
  • 30
    • 71749097244 scopus 로고    scopus 로고
    • Purification and reconstitution of the antigen transport complex TAP: A prerequisite for determination of peptide stoichiometry and ATP hydrolysis
    • Herget, M. et al. Purification and reconstitution of the antigen transport complex TAP: a prerequisite for determination of peptide stoichiometry and ATP hydrolysis. J. Biol. Chem. 284, 33740-33749 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 33740-33749
    • Herget, M.1
  • 31
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter, P. & Ron, D. The unfolded protein response: from stress pathway to homeostatic regulation. Science 334, 1081-1086 (2011).
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 32
    • 77952709552 scopus 로고    scopus 로고
    • Single residue within the antigen translocation complex TAP controls the epitope repertoire by stabilizing a receptive conformation
    • Baldauf, C., Schrodt, S., Herget, M., Koch, J. & Tampé, R. Single residue within the antigen translocation complex TAP controls the epitope repertoire by stabilizing a receptive conformation. Proc. Natl Acad. Sci. USA 107, 9135-9140 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 9135-9140
    • Baldauf, C.1    Schrodt, S.2    Herget, M.3    Koch, J.4    Tampé, R.5
  • 33
    • 80053091327 scopus 로고    scopus 로고
    • Snapshots of the maltose transporter during ATP hydrolysis
    • Oldham, M. L. & Chen, J. Snapshots of the maltose transporter during ATP hydrolysis. Proc. Natl Acad. Sci. USA 108, 15152-15156 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 15152-15156
    • Oldham, M.L.1    Chen, J.2
  • 34
    • 84867670628 scopus 로고    scopus 로고
    • Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F
    • Korkhov, V. M., Mireku, S. A. & Locher, K. P. Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F. Nature 490, 367-372 (2012).
    • (2012) Nature , vol.490 , pp. 367-372
    • Korkhov, V.M.1    Mireku, S.A.2    Locher, K.P.3
  • 35
    • 84858767204 scopus 로고    scopus 로고
    • Role of the D-loops in allosteric control of ATP hydrolysis in an ABC transporter
    • Jones, P. M. & George, A. M. Role of the D-loops in allosteric control of ATP hydrolysis in an ABC transporter. J. Phys. Chem. A 116, 3004-3013 (2012).
    • (2012) J. Phys. Chem. A , vol.116 , pp. 3004-3013
    • Jones, P.M.1    George, A.M.2
  • 36
    • 84905040016 scopus 로고    scopus 로고
    • Structural basis for allosteric cross-talk between the asymmetric nucleotide binding sites of a heterodimeric ABC exporter
    • Hohl, M. et al. Structural basis for allosteric cross-talk between the asymmetric nucleotide binding sites of a heterodimeric ABC exporter. Proc. Natl Acad. Sci. USA 111, 11025-11030 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 11025-11030
    • Hohl, M.1
  • 38
    • 0029148985 scopus 로고
    • Requirements for peptide binding to the human transporter associated with antigen processing revealed by peptide scans and complex peptide libraries
    • Uebel, S. et al. Requirements for peptide binding to the human transporter associated with antigen processing revealed by peptide scans and complex peptide libraries. J. Biol. Chem. 270, 18512-18516 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 18512-18516
    • Uebel, S.1
  • 39
    • 84891393628 scopus 로고    scopus 로고
    • Analyses of conformational states of the transporter associated with antigen processing (TAP) in a native cellular membrane environment
    • Geng, J., Sivaramakrishnan, S. & Raghavan, M. Analyses of conformational states of the transporter associated with antigen processing (TAP) in a native cellular membrane environment. J. Biol. Chem. 288, 37039-37047 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 37039-37047
    • Geng, J.1    Sivaramakrishnan, S.2    Raghavan, M.3
  • 40
    • 84870316798 scopus 로고    scopus 로고
    • Molecular architecture of the MHC i peptide-loading complex: One tapasin molecule is essential and sufficient for antigen processing
    • Hulpke, S., Baldauf, C. & Tampé, R. Molecular architecture of the MHC I peptide-loading complex: one tapasin molecule is essential and sufficient for antigen processing. FASEB J. 26, 5071-5080 (2012).
    • (2012) FASEB J. , vol.26 , pp. 5071-5080
    • Hulpke, S.1    Baldauf, C.2    Tampé, R.3
  • 41
    • 44349100345 scopus 로고    scopus 로고
    • Functionally important interactions between the nucleotide-binding domains of an antigenic peptide transporter
    • Procko, E. & Gaudet, R. Functionally important interactions between the nucleotide-binding domains of an antigenic peptide transporter. Biochemistry 47, 5699-5708 (2008).
    • (2008) Biochemistry , vol.47 , pp. 5699-5708
    • Procko, E.1    Gaudet, R.2
  • 42
    • 0028110959 scopus 로고
    • Functional expression and purification of the ABC transporter complex associated with antigen processing (TAP) in insect cells
    • Meyer, T. H., van Endert, P. M., Uebel, S., Ehring, B. & Tampé, R. Functional expression and purification of the ABC transporter complex associated with antigen processing (TAP) in insect cells. FEBS Lett. 351, 443-447 (1994).
    • (1994) FEBS Lett. , vol.351 , pp. 443-447
    • Meyer, T.H.1    Van Endert, P.M.2    Uebel, S.3    Ehring, B.4    Tampé, R.5
  • 43
    • 0028501327 scopus 로고
    • A sequential model for peptide binding and transport by the transporters associated with antigen processing
    • van Endert, P. M. et al. A sequential model for peptide binding and transport by the transporters associated with antigen processing. Immunity 1, 491-500 (1994).
    • (1994) Immunity , vol.1 , pp. 491-500
    • Van Endert, P.M.1
  • 44
    • 84866114976 scopus 로고    scopus 로고
    • Direct evidence that the N-terminal extensions of the TAP complex act as autonomous interaction scaffolds for the assembly of the MHC i peptide-loading complex
    • Hulpke, S. et al. Direct evidence that the N-terminal extensions of the TAP complex act as autonomous interaction scaffolds for the assembly of the MHC I peptide-loading complex. Cell. Mol. Life Sci. 69, 3317-3327 (2012).
    • (2012) Cell. Mol. Life Sci. , vol.69 , pp. 3317-3327
    • Hulpke, S.1
  • 46
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 47
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. 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. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 48
    • 0034655949 scopus 로고    scopus 로고
    • The morph server: A standardized system for analyzing and visualizing macromolecular motions in a database framework
    • Krebs, W. G. & Gerstein, M. The morph server: a standardized system for analyzing and visualizing macromolecular motions in a database framework. Nucleic Acids Res. 28, 1665-1675 (2000).
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1665-1675
    • Krebs, W.G.1    Gerstein, M.2
  • 50
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: A tutorial review
    • Lebowitz, J., Lewis, M. S. & Schuck, P. Modern analytical ultracentrifugation in protein science: a tutorial review. Protein Sci. 11, 2067-2079 (2002).
    • (2002) Protein Sci. , vol.11 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 51
    • 1442274756 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition
    • Vistica, J. et al. Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition. Anal. Biochem. 326, 234-256 (2004).
    • (2004) Anal. Biochem. , vol.326 , pp. 234-256
    • Vistica, J.1


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