메뉴 건너뛰기




Volumn 1778, Issue 9, 2008, Pages 1805-1813

A perspective on the structural studies of inner membrane electrochemical potential-driven transporters

Author keywords

AcrB; DAACS; EmrD; GlpT; GltPh; LacY; LeuT; Membrane protein; NhaA; Structural biology; Transporter; X ray crystallography

Indexed keywords

CARRIER PROTEIN; MEMBRANE PROTEIN;

EID: 50049105844     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.01.009     Document Type: Review
Times cited : (6)

References (40)
  • 1
    • 0021895119 scopus 로고
    • Pi exchange mediated by the GlpT-dependent sn-glycerol-3-phosphate transport system in Escherichia coli
    • Elvin C.M., Hardy C.M., and Rosenberg H. Pi exchange mediated by the GlpT-dependent sn-glycerol-3-phosphate transport system in Escherichia coli. J. Bacteriol. 161 (1985) 1054-1058
    • (1985) J. Bacteriol. , vol.161 , pp. 1054-1058
    • Elvin, C.M.1    Hardy, C.M.2    Rosenberg, H.3
  • 2
    • 0023000305 scopus 로고
    • Reconstitution of sugar phosphate transport systems of Escherichia coli
    • Ambudkar S.V., Larson T.J., and Maloney P.C. Reconstitution of sugar phosphate transport systems of Escherichia coli. J. Biol. Chem. 261 (1986) 9083-9086
    • (1986) J. Biol. Chem. , vol.261 , pp. 9083-9086
    • Ambudkar, S.V.1    Larson, T.J.2    Maloney, P.C.3
  • 3
    • 4544231184 scopus 로고    scopus 로고
    • Glycerol-3-phosphate transporter of Escherichia coli: structure, function and regulation
    • Lemieux M.J., Huang Y., and Wang D.N. Glycerol-3-phosphate transporter of Escherichia coli: structure, function and regulation. Res. Microbiol. 155 (2004) 623-629
    • (2004) Res. Microbiol. , vol.155 , pp. 623-629
    • Lemieux, M.J.1    Huang, Y.2    Wang, D.N.3
  • 5
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Huang Y., Lemieux M.J., Song J., Auer M., and Wang D.N. Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301 (2003) 616-620
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 6
    • 0345276579 scopus 로고    scopus 로고
    • Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily
    • Lemieux M.J., Song J., Kim M.J., Huang Y., Villa A., Auer M., Li X.D., and Wang D.N. Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily. Protein Sci. 12 (2003) 2748-2756
    • (2003) Protein Sci. , vol.12 , pp. 2748-2756
    • Lemieux, M.J.1    Song, J.2    Kim, M.J.3    Huang, Y.4    Villa, A.5    Auer, M.6    Li, X.D.7    Wang, D.N.8
  • 8
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson J., Smirnova I., Kasho V., Verner G., Kaback H.R., and Iwata S. Structure and mechanism of the lactose permease of Escherichia coli. Science 301 (2003) 610-615
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 9
    • 33645320817 scopus 로고    scopus 로고
    • Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY
    • Mirza O., Guan L., Verner G., Iwata S., and Kaback H.R. Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY. Embo J. 25 (2006) 1177-1183
    • (2006) Embo J. , vol.25 , pp. 1177-1183
    • Mirza, O.1    Guan, L.2    Verner, G.3    Iwata, S.4    Kaback, H.R.5
  • 10
    • 0037452911 scopus 로고    scopus 로고
    • A mutation in the lactose permease of Escherichia coli that decreases conformational flexibility and increases protein stability
    • Smirnova I.N., and Kaback H.R. A mutation in the lactose permease of Escherichia coli that decreases conformational flexibility and increases protein stability. Biochemistry 42 (2003) 3025-3031
    • (2003) Biochemistry , vol.42 , pp. 3025-3031
    • Smirnova, I.N.1    Kaback, H.R.2
  • 12
    • 33646445156 scopus 로고    scopus 로고
    • Structure of the multidrug transporter EmrD from Escherichia coli
    • Yin Y., He X., Szewczyk P., Nguyen T., and Chang G. Structure of the multidrug transporter EmrD from Escherichia coli. Science 312 (2006) 741-744
    • (2006) Science , vol.312 , pp. 741-744
    • Yin, Y.1    He, X.2    Szewczyk, P.3    Nguyen, T.4    Chang, G.5
  • 13
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami S., Nakashima R., Yamashita E., and Yamaguchi A. Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419 (2002) 587-593
    • (2002) Nature , vol.419 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 14
    • 0038670226 scopus 로고    scopus 로고
    • Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump
    • Yu E.W., McDermott G., Zgurskaya H.I., Nikaido H., and Koshland Jr. D.E. Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump. Science 300 (2003) 976-980
    • (2003) Science , vol.300 , pp. 976-980
    • Yu, E.W.1    McDermott, G.2    Zgurskaya, H.I.3    Nikaido, H.4    Koshland Jr., D.E.5
  • 15
    • 33748670458 scopus 로고    scopus 로고
    • Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
    • Murakami S., Nakashima R., Yamashita E., Matsumoto T., and Yamaguchi A. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature 443 (2006) 173-179
    • (2006) Nature , vol.443 , pp. 173-179
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Matsumoto, T.4    Yamaguchi, A.5
  • 16
    • 33748310520 scopus 로고    scopus 로고
    • Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism
    • Seeger M.A., Schiefner A., Eicher T., Verrey F., Diederichs K., and Pos K.M. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science 313 (2006) 1295-1298
    • (2006) Science , vol.313 , pp. 1295-1298
    • Seeger, M.A.1    Schiefner, A.2    Eicher, T.3    Verrey, F.4    Diederichs, K.5    Pos, K.M.6
  • 17
    • 0036046157 scopus 로고    scopus 로고
    • Monoamine transporter gene structure and polymorphisms in relation to psychiatric and other complex disorders
    • Hahn M.K., and Blakely R.D. Monoamine transporter gene structure and polymorphisms in relation to psychiatric and other complex disorders. Pharmacogenomics J. 2 (2002) 217-235
    • (2002) Pharmacogenomics J. , vol.2 , pp. 217-235
    • Hahn, M.K.1    Blakely, R.D.2
  • 18
    • 24644470065 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of Na+/Cl- dependent neurotransmitter transporters
    • Yamashita A., Singh S.K., Kawate T., Jin Y., and Gouaux E. Crystal structure of a bacterial homologue of Na+/Cl- dependent neurotransmitter transporters. Nature 437 (2005) 215-223
    • (2005) Nature , vol.437 , pp. 215-223
    • Yamashita, A.1    Singh, S.K.2    Kawate, T.3    Jin, Y.4    Gouaux, E.5
  • 19
    • 34548178234 scopus 로고    scopus 로고
    • Antidepressant binding site in a bacterial homologue of neurotransmitter transporters
    • Singh S.K., Yamashita A., and Gouaux E. Antidepressant binding site in a bacterial homologue of neurotransmitter transporters. Nature 448 (2007) 952-956
    • (2007) Nature , vol.448 , pp. 952-956
    • Singh, S.K.1    Yamashita, A.2    Gouaux, E.3
  • 21
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., and Walker J.E. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260 (1996) 289-298
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 22
  • 23
    • 0242424106 scopus 로고    scopus 로고
    • Trimeric subunit stoichiometry of the glutamate transporters from Bacillus caldotenax and Bacillus stearothermophilus
    • Yernool D., Boudker O., Folta-Stogniew E., and Gouaux E. Trimeric subunit stoichiometry of the glutamate transporters from Bacillus caldotenax and Bacillus stearothermophilus. Biochemistry 42 (2003) 12981-12988
    • (2003) Biochemistry , vol.42 , pp. 12981-12988
    • Yernool, D.1    Boudker, O.2    Folta-Stogniew, E.3    Gouaux, E.4
  • 24
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • Yernool D., Boudker O., Jin Y., and Gouaux E. Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431 (2004) 811-818
    • (2004) Nature , vol.431 , pp. 811-818
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4
  • 25
    • 33846505059 scopus 로고    scopus 로고
    • Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter
    • Boudker O., Ryan R.M., Yernool D., Shimamoto K., and Gouaux E. Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter. Nature 445 (2007) 387-393
    • (2007) Nature , vol.445 , pp. 387-393
    • Boudker, O.1    Ryan, R.M.2    Yernool, D.3    Shimamoto, K.4    Gouaux, E.5
  • 26
    • 33947531619 scopus 로고    scopus 로고
    • Physiological role and regulation of the Na+/H+ exchanger
    • Malo M.E., and Fliegel L. Physiological role and regulation of the Na+/H+ exchanger. Can. J. Physiol. Pharmacol. 84 (2006) 1081-1095
    • (2006) Can. J. Physiol. Pharmacol. , vol.84 , pp. 1081-1095
    • Malo, M.E.1    Fliegel, L.2
  • 27
    • 0025964976 scopus 로고
    • Identification of the protein and cDNA of the cardiac Na+/H+ exchanger
    • Fliegel L., Sardet C., Pouyssegur J., and Barr A. Identification of the protein and cDNA of the cardiac Na+/H+ exchanger. FEBS Lett. 279 (1991) 25-29
    • (1991) FEBS Lett. , vol.279 , pp. 25-29
    • Fliegel, L.1    Sardet, C.2    Pouyssegur, J.3    Barr, A.4
  • 28
    • 0037353993 scopus 로고    scopus 로고
    • The role of endogenous angiotensin II in ischaemia, reperfusion and preconditioning of the isolated rat heart
    • Xiao X.H., and Allen D.G. The role of endogenous angiotensin II in ischaemia, reperfusion and preconditioning of the isolated rat heart. Pflugers Arch. 445 (2003) 643-650
    • (2003) Pflugers Arch. , vol.445 , pp. 643-650
    • Xiao, X.H.1    Allen, D.G.2
  • 29
    • 33947582886 scopus 로고    scopus 로고
    • Sodium-hydrogen exchanger, cardiac overload, and myocardial hypertrophy
    • Cingolani H.E., and Ennis I.L. Sodium-hydrogen exchanger, cardiac overload, and myocardial hypertrophy. Circulation 115 9 (2007) 1090-1100
    • (2007) Circulation , vol.115 , Issue.9 , pp. 1090-1100
    • Cingolani, H.E.1    Ennis, I.L.2
  • 30
    • 21744436321 scopus 로고    scopus 로고
    • Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH
    • Hunte C., Screpanti E., Venturi M., Rimon A., Padan E., and Michel H. Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH. Nature 435 (2005) 1197-1202
    • (2005) Nature , vol.435 , pp. 1197-1202
    • Hunte, C.1    Screpanti, E.2    Venturi, M.3    Rimon, A.4    Padan, E.5    Michel, H.6
  • 31
    • 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
  • 33
    • 0024117785 scopus 로고
    • Three-dimensional crystallization of membrane proteins.
    • Kühlbrandt W. Three-dimensional crystallization of membrane proteins. Quart. Rev. Biophys. 21 (1988) 429-477
    • (1988) Quart. Rev. Biophys. , vol.21 , pp. 429-477
    • Kühlbrandt, W.1
  • 34
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
    • Toyoshima C., Nakasako M., Nomura H., and Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature 405 (2000) 647-655
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 35
    • 0036427425 scopus 로고    scopus 로고
    • Importance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain
    • Lemieux M.J., Reithmeier R.A., and Wang D.N. Importance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain. J. Struct. Biol. 137 (2002) 322-332
    • (2002) J. Struct. Biol. , vol.137 , pp. 322-332
    • Lemieux, M.J.1    Reithmeier, R.A.2    Wang, D.N.3
  • 36
    • 34548099721 scopus 로고    scopus 로고
    • Eukaryotic major facilitator superfamily transporter modeling based on the prokaryotic GlpT crystal structure (Review)
    • Lemieux M.J. Eukaryotic major facilitator superfamily transporter modeling based on the prokaryotic GlpT crystal structure (Review). Mol. Membr. Biol. 24 (2007) 333-341
    • (2007) Mol. Membr. Biol. , vol.24 , pp. 333-341
    • Lemieux, M.J.1
  • 37
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long S.B., Campbell E.B., and Mackinnon R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309 (2005) 897-903
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 40
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel
    • Chang G., Spencer R.H., Lee A.T., Barclay M.T., and Rees D.C. Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science 282 (1998) 2220-2226
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.