메뉴 건너뛰기




Volumn 22, Issue 5, 2014, Pages 769-780

Extracellular loop 4 of the proline transporter PutP controls the periplasmic entrance to ligand binding sites

Author keywords

[No Author keywords available]

Indexed keywords

COTRANSPORTER; EXTRACELLULAR LOOP 4; MEMBRANE PROTEIN; PROLINE SYMPORTER; UNCLASSIFIED DRUG; AMINO ACID TRANSPORTER; ESCHERICHIA COLI PROTEIN; LIGAND; PHENYLALANINE; PUTP PROTEIN, E COLI;

EID: 84899911642     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.03.011     Document Type: Article
Times cited : (19)

References (64)
  • 1
    • 0025346254 scopus 로고
    • Transmembrane protein structure: Spin labeling of bacteriorhodopsin mutants
    • C. Altenbach, T. Marti, H.G. Khorana, and W.L. Hubbell Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants Science 248 1990 1088 1092
    • (1990) Science , vol.248 , pp. 1088-1092
    • Altenbach, C.1    Marti, T.2    Khorana, H.G.3    Hubbell, W.L.4
  • 2
    • 24144502337 scopus 로고    scopus 로고
    • Accessibility of nitroxide side chains: Absolute Heisenberg exchange rates from power saturation EPR
    • C. Altenbach, W. Froncisz, R. Hemker, H. McHaourab, and W.L. Hubbell Accessibility of nitroxide side chains: absolute Heisenberg exchange rates from power saturation EPR Biophys. J. 89 2005 2103 2112
    • (2005) Biophys. J. , vol.89 , pp. 2103-2112
    • Altenbach, C.1    Froncisz, W.2    Hemker, R.3    McHaourab, H.4    Hubbell, W.L.5
  • 3
    • 0032912746 scopus 로고    scopus 로고
    • Impact of the high-affinity proline permease gene (putP) on the virulence of Staphylococcus aureus in experimental endocarditis
    • A.S. Bayer, S.N. Coulter, C.K. Stover, and W.R. Schwan Impact of the high-affinity proline permease gene (putP) on the virulence of Staphylococcus aureus in experimental endocarditis Infect. Immun. 67 1999 740 744
    • (1999) Infect. Immun. , vol.67 , pp. 740-744
    • Bayer, A.S.1    Coulter, S.N.2    Stover, C.K.3    Schwan, W.R.4
  • 4
    • 61349166815 scopus 로고    scopus 로고
    • Membrane protein structure and dynamics studied by site-directed spin labeling ESR
    • M.A. Hemminga, L.J. Berliner, Springer New York
    • E. Bordignon, and H.-J. Steinhoff Membrane protein structure and dynamics studied by site-directed spin labeling ESR M.A. Hemminga, L.J. Berliner, ESR Spectroscopy in Membrane Biophysics 2007 Springer New York 129 164
    • (2007) ESR Spectroscopy in Membrane Biophysics , pp. 129-164
    • Bordignon, E.1    Steinhoff, H.-J.2
  • 5
    • 84881430324 scopus 로고    scopus 로고
    • Coupled global and local changes direct substrate translocation by neurotransmitter-sodium symporter ortholog LeuT
    • M.H. Cheng, and I. Bahar Coupled global and local changes direct substrate translocation by neurotransmitter-sodium symporter ortholog LeuT Biophys. J. 105 2013 630 639
    • (2013) Biophys. J. , vol.105 , pp. 630-639
    • Cheng, M.H.1    Bahar, I.2
  • 9
    • 73949083478 scopus 로고    scopus 로고
    • The rocking bundle: A mechanism for ion-coupled solute flux by symmetrical transporters
    • L.R. Forrest, and G. Rudnick The rocking bundle: a mechanism for ion-coupled solute flux by symmetrical transporters Physiology (Bethesda) 24 2009 377 386
    • (2009) Physiology (Bethesda) , vol.24 , pp. 377-386
    • Forrest, L.R.1    Rudnick, G.2
  • 11
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • N. Guex, and M.C. Peitsch SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 13
    • 41949124711 scopus 로고    scopus 로고
    • +/proline transporter PutP of Escherichia coli in ligand binding and transport
    • +/proline transporter PutP of Escherichia coli in ligand binding and transport J. Biol. Chem. 283 2008 4921 4929
    • (2008) J. Biol. Chem. , vol.283 , pp. 4921-4929
    • Hilger, D.1    Böhm, M.2    Hackmann, A.3    Jung, H.4
  • 16
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • W.L. Hubbell, D.S. Cafiso, and C. Altenbach Identifying conformational changes with site-directed spin labeling Nat. Struct. Biol. 7 2000 735 739
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 17
    • 0037022173 scopus 로고    scopus 로고
    • Structure and dynamics of a helical hairpin and loop region in annexin 12: A site-directed spin labeling study
    • J.M. Isas, R. Langen, H.T. Haigler, and W.L. Hubbell Structure and dynamics of a helical hairpin and loop region in annexin 12: a site-directed spin labeling study Biochemistry 41 2002 1464 1473
    • (2002) Biochemistry , vol.41 , pp. 1464-1473
    • Isas, J.M.1    Langen, R.2    Haigler, H.T.3    Hubbell, W.L.4
  • 18
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • O. Jardetzky Simple allosteric model for membrane pumps Nature 211 1966 969 970
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 19
    • 84859888767 scopus 로고    scopus 로고
    • DEER distance measurements on proteins
    • G. Jeschke DEER distance measurements on proteins Annu. Rev. Phys. Chem. 63 2012 419 446
    • (2012) Annu. Rev. Phys. Chem. , vol.63 , pp. 419-446
    • Jeschke, G.1
  • 20
    • 84877303485 scopus 로고    scopus 로고
    • A comparative study of structures and structural transitions of secondary transporters with the LeuT fold
    • G. Jeschke A comparative study of structures and structural transitions of secondary transporters with the LeuT fold Eur. Biophys. J. 42 2013 181 197
    • (2013) Eur. Biophys. J. , vol.42 , pp. 181-197
    • Jeschke, G.1
  • 21
    • 34147218123 scopus 로고    scopus 로고
    • Distance measurements on spin-labelled biomacromolecules by pulsed electron paramagnetic resonance
    • G. Jeschke, and Y. Polyhach Distance measurements on spin-labelled biomacromolecules by pulsed electron paramagnetic resonance Phys. Chem. Chem. Phys. 9 2007 1895 1910
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 1895-1910
    • Jeschke, G.1    Polyhach, Y.2
  • 25
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander 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
  • 28
    • 84856225222 scopus 로고    scopus 로고
    • X-ray structures of LeuT in substrate-free outward-open and apo inward-open states
    • H. Krishnamurthy, and E. Gouaux X-ray structures of LeuT in substrate-free outward-open and apo inward-open states Nature 481 2012 469 474
    • (2012) Nature , vol.481 , pp. 469-474
    • Krishnamurthy, H.1    Gouaux, E.2
  • 29
    • 70450106216 scopus 로고    scopus 로고
    • Improved prediction of protein side-chain conformations with SCWRL4
    • G.G. Krivov, M.V. Shapovalov, and R.L. Dunbrack Jr. Improved prediction of protein side-chain conformations with SCWRL4 Proteins 77 2009 778 795
    • (2009) Proteins , vol.77 , pp. 778-795
    • Krivov, G.G.1    Shapovalov, M.V.2    Dunbrack, Jr.R.L.3
  • 31
    • 0039171268 scopus 로고    scopus 로고
    • Crystal structures of spin labeled T4 lysozyme mutants: Implications for the interpretation of EPR spectra in terms of structure
    • R. Langen, K.J. Oh, D. Cascio, and W.L. Hubbell Crystal structures of spin labeled T4 lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure Biochemistry 39 2000 8396 8405
    • (2000) Biochemistry , vol.39 , pp. 8396-8405
    • Langen, R.1    Oh, K.J.2    Cascio, D.3    Hubbell, W.L.4
  • 32
    • 84862819559 scopus 로고    scopus 로고
    • Structure and mechanism of a glutamate-GABA antiporter
    • D. Ma, P. Lu, C. Yan, C. Fan, P. Yin, J. Wang, and Y. Shi Structure and mechanism of a glutamate-GABA antiporter Nature 483 2012 632 636
    • (2012) Nature , vol.483 , pp. 632-636
    • Ma, D.1    Lu, P.2    Yan, C.3    Fan, C.4    Yin, P.5    Wang, J.6    Shi, Y.7
  • 33
    • 0032476844 scopus 로고    scopus 로고
    • Determination of end-to-end distances in a series of TEMPO diradicals of up to 2.8 nm length with a new four-pulse double electron electron resonance experiment
    • R.E. Martin, M. Pannier, F. Diederich, V. Gramlich, M. Hubrich, and H.W. Spiess Determination of end-to-end distances in a series of TEMPO diradicals of up to 2.8 nm length with a new four-pulse double electron electron resonance experiment Angewandte Chemie International Edition 37 1998 2833 2837
    • (1998) Angewandte Chemie International Edition , vol.37 , pp. 2833-2837
    • Martin, R.E.1    Pannier, M.2    Diederich, F.3    Gramlich, V.4    Hubrich, M.5    Spiess, H.W.6
  • 34
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • H.S. Mchaourab, M.A. Lietzow, K. Hideg, and W.L. Hubbell 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
  • 35
    • 2642549055 scopus 로고    scopus 로고
    • Structure and function of extracellular loop 4 of the serotonin transporter as revealed by cysteine-scanning mutagenesis
    • S.M. Mitchell, E. Lee, M.L. Garcia, and M.M. Stephan Structure and function of extracellular loop 4 of the serotonin transporter as revealed by cysteine-scanning mutagenesis J. Biol. Chem. 279 2004 24089 24099
    • (2004) J. Biol. Chem. , vol.279 , pp. 24089-24099
    • Mitchell, S.M.1    Lee, E.2    Garcia, M.L.3    Stephan, M.M.4
  • 37
    • 0034132251 scopus 로고    scopus 로고
    • Dead-time free measurement of dipole-dipole interactions between electron spins
    • M. Pannier, S. Veit, A. Godt, G. Jeschke, and H.W. Spiess Dead-time free measurement of dipole-dipole interactions between electron spins J. Magn. Reson. 142 2000 331 340
    • (2000) J. Magn. Reson. , vol.142 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Godt, A.3    Jeschke, G.4    Spiess, H.W.5
  • 38
    • 84887404259 scopus 로고    scopus 로고
    • X-ray structure of dopamine transporter elucidates antidepressant mechanism
    • A. Penmatsa, K.H. Wang, and E. Gouaux X-ray structure of dopamine transporter elucidates antidepressant mechanism Nature 503 2013 85 90
    • (2013) Nature , vol.503 , pp. 85-90
    • Penmatsa, A.1    Wang, K.H.2    Gouaux, E.3
  • 39
    • 84867092080 scopus 로고    scopus 로고
    • Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP
    • C. Perez, C. Koshy, O. Yildiz, and C. Ziegler Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP Nature 490 2012 126 130
    • (2012) Nature , vol.490 , pp. 126-130
    • Perez, C.1    Koshy, C.2    Yildiz, O.3    Ziegler, C.4
  • 40
    • 0242290359 scopus 로고    scopus 로고
    • +/proline transporter PutP of Escherichia coli forms part of a conformationally flexible, cytoplasmic exposed aqueous cavity within the membrane
    • +/proline transporter PutP of Escherichia coli forms part of a conformationally flexible, cytoplasmic exposed aqueous cavity within the membrane J. Biol. Chem. 278 2003 42942 42949
    • (2003) J. Biol. Chem. , vol.278 , pp. 42942-42949
    • Pirch, T.1    Landmeier, S.2    Jung, H.3
  • 41
    • 0037059138 scopus 로고    scopus 로고
    • Molecular orbital study of polarity and hydrogen bonding effects on the g and hyperfine tensors of site directed NO spin labeled bacteriorhodopsin
    • M. Plato, H.J. Steinhoff, C. Wegener, J.T. Törring, A. Savitsky, and K. Möbius Molecular orbital study of polarity and hydrogen bonding effects on the g and hyperfine tensors of site directed NO spin labeled bacteriorhodopsin Mol. Phys. 100 2002 3711 3721
    • (2002) Mol. Phys. , vol.100 , pp. 3711-3721
    • Plato, M.1    Steinhoff, H.J.2    Wegener, C.3    Törring, J.T.4    Savitsky, A.5    Möbius, K.6
  • 42
    • 79251562868 scopus 로고    scopus 로고
    • Rotamer libraries of spin labelled cysteines for protein studies
    • Y. Polyhach, E. Bordignon, and G. Jeschke Rotamer libraries of spin labelled cysteines for protein studies Phys. Chem. Chem. Phys. 13 2011 2356 2366
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 2356-2366
    • Polyhach, Y.1    Bordignon, E.2    Jeschke, G.3
  • 43
    • 84863966856 scopus 로고    scopus 로고
    • High sensitivity and versatility of the DEER experiment on nitroxide radical pairs at Q-band frequencies
    • Y. Polyhach, E. Bordignon, R. Tschaggelar, S. Gandra, A. Godt, and G. Jeschke High sensitivity and versatility of the DEER experiment on nitroxide radical pairs at Q-band frequencies Phys. Chem. Chem. Phys. 14 2012 10762 10773
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 10762-10773
    • Polyhach, Y.1    Bordignon, E.2    Tschaggelar, R.3    Gandra, S.4    Godt, A.5    Jeschke, G.6
  • 44
    • 33847675341 scopus 로고    scopus 로고
    • Monitoring the function of membrane transport proteins in detergent-solubilized form
    • M. Quick, and J.A. Javitch Monitoring the function of membrane transport proteins in detergent-solubilized form Proc. Natl. Acad. Sci. USA 104 2007 3603 3608
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 3603-3608
    • Quick, M.1    Javitch, J.A.2
  • 45
    • 0030887995 scopus 로고    scopus 로고
    • +-coupled proline uptake
    • +-coupled proline uptake Biochemistry 36 1997 4631 4636
    • (1997) Biochemistry , vol.36 , pp. 4631-4636
    • Quick, M.1    Jung, H.2
  • 46
    • 0029957853 scopus 로고    scopus 로고
    • +/proline permease of Escherichia coli is critical for high-affinity proline uptake
    • +/proline permease of Escherichia coli is critical for high-affinity proline uptake Eur. J. Biochem. 239 1996 732 736
    • (1996) Eur. J. Biochem. , vol.239 , pp. 732-736
    • Quick, M.1    Tebbe, S.2    Jung, H.3
  • 48
    • 44249090228 scopus 로고    scopus 로고
    • Molecular characterization of V59E NIS, a Na+/I- symporter mutant that causes congenital I- transport defect
    • M.D. Reed-Tsur, A. De la Vieja, C.S. Ginter, and N. Carrasco Molecular characterization of V59E NIS, a Na+/I- symporter mutant that causes congenital I- transport defect Endocrinology 149 2008 3077 3084
    • (2008) Endocrinology , vol.149 , pp. 3077-3084
    • Reed-Tsur, M.D.1    De La Vieja, A.2    Ginter, C.S.3    Carrasco, N.4
  • 50
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • A. Sali, and T.L. Blundell Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234 1993 779 815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 54
    • 80755122853 scopus 로고    scopus 로고
    • Lactose permease and the alternating access mechanism
    • I. Smirnova, V. Kasho, and H.R. Kaback Lactose permease and the alternating access mechanism Biochemistry 50 2011 9684 9693
    • (2011) Biochemistry , vol.50 , pp. 9684-9693
    • Smirnova, I.1    Kasho, V.2    Kaback, H.R.3
  • 55
    • 0021031927 scopus 로고
    • Two proline porters in Escherichia coli K-12
    • M.E. Stalmach, S. Grothe, and J.M. Wood Two proline porters in Escherichia coli K-12 J. Bacteriol. 156 1983 481 486
    • (1983) J. Bacteriol. , vol.156 , pp. 481-486
    • Stalmach, M.E.1    Grothe, S.2    Wood, J.M.3
  • 56
    • 0030781782 scopus 로고    scopus 로고
    • Determination of interspin distances between spin labels attached to insulin: Comparison of electron paramagnetic resonance data with the X-ray structure
    • H.J. Steinhoff, N. Radzwill, W. Thevis, V. Lenz, D. Brandenburg, A. Antson, G. Dodson, and A. Wollmer Determination of interspin distances between spin labels attached to insulin: comparison of electron paramagnetic resonance data with the X-ray structure Biophys. J. 73 1997 3287 3298
    • (1997) Biophys. J. , vol.73 , pp. 3287-3298
    • Steinhoff, H.J.1    Radzwill, N.2    Thevis, W.3    Lenz, V.4    Brandenburg, D.5    Antson, A.6    Dodson, G.7    Wollmer, A.8
  • 57
    • 0034639884 scopus 로고    scopus 로고
    • High-field EPR studies of the structure and conformational changes of site-directed spin labeled bacteriorhodopsin
    • H.J. Steinhoff, A. Savitsky, C. Wegener, M. Pfeiffer, M. Plato, and K. Möbius High-field EPR studies of the structure and conformational changes of site-directed spin labeled bacteriorhodopsin Biochim. Biophys. Acta 1457 2000 253 262
    • (2000) Biochim. Biophys. Acta , vol.1457 , pp. 253-262
    • Steinhoff, H.J.1    Savitsky, A.2    Wegener, C.3    Pfeiffer, M.4    Plato, M.5    Möbius, K.6
  • 59
    • 0034712685 scopus 로고    scopus 로고
    • Spin labeling analysis of structure and dynamics of the Na+/proline transporter of Escherichia coli
    • C. Wegener, S. Tebbe, H.J. Steinhoff, and H. Jung Spin labeling analysis of structure and dynamics of the Na+/proline transporter of Escherichia coli Biochemistry 39 2000 4831 4837
    • (2000) Biochemistry , vol.39 , pp. 4831-4837
    • Wegener, C.1    Tebbe, S.2    Steinhoff, H.J.3    Jung, H.4
  • 61
    • 1242272759 scopus 로고    scopus 로고
    • The sodium/glucose cotransport family SLC5
    • E.M. Wright, and E. Turk The sodium/glucose cotransport family SLC5 Pflugers Arch. 447 2004 510 518
    • (2004) Pflugers Arch. , vol.447 , pp. 510-518
    • Wright, E.M.1    Turk, E.2
  • 62
    • 33846023326 scopus 로고    scopus 로고
    • Active sugar transport in health and disease
    • E.M. Wright, B.A. Hirayama, and D.F. Loo Active sugar transport in health and disease J. Intern. Med. 261 2007 32 43
    • (2007) J. Intern. Med. , vol.261 , pp. 32-43
    • Wright, E.M.1    Hirayama, B.A.2    Loo, D.F.3
  • 64
    • 0242353345 scopus 로고    scopus 로고
    • The interaction of the γ-aminobutyric acid transporter GAT-1 with the neurotransmitter is selectively impaired by sulfhydryl modification of a conformationally sensitive cysteine residue engineered into extracellular loop IV
    • E. Zomot, and B.I. Kanner The interaction of the γ-aminobutyric acid transporter GAT-1 with the neurotransmitter is selectively impaired by sulfhydryl modification of a conformationally sensitive cysteine residue engineered into extracellular loop IV J. Biol. Chem. 278 2003 42950 42958
    • (2003) J. Biol. Chem. , vol.278 , pp. 42950-42958
    • Zomot, E.1    Kanner, B.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.