메뉴 건너뛰기




Volumn 21, Issue 7, 2013, Pages 1243-1250

Structure and substrate-induced conformational changes of the secondary citrate/sodium symporter CitS revealed by electron crystallography

Author keywords

[No Author keywords available]

Indexed keywords

CITRATE SODIUM; CITRATE SODIUM SYMPORTER; CITRIC ACID; DIMER; MONOMER; PROTEIN; SODIUM; UNCLASSIFIED DRUG;

EID: 84879839641     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.05.011     Document Type: Article
Times cited : (11)

References (39)
  • 1
    • 69249136609 scopus 로고    scopus 로고
    • Structure and function of Na(+)-symporters with inverted repeats
    • J. Abramson, and E.M. Wright Structure and function of Na(+)-symporters with inverted repeats Curr. Opin. Struct. Biol. 19 2009 425 432
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 425-432
    • Abramson, J.1    Wright, E.M.2
  • 2
    • 64649100382 scopus 로고    scopus 로고
    • Conformations of NhaA, the Na+/H+ exchanger from Escherichia coli, in the pH-activated and ion-translocating states
    • M. Appel, D. Hizlan, K.R. Vinothkumar, C. Ziegler, and W. Kühlbrandt Conformations of NhaA, the Na+/H+ exchanger from Escherichia coli, in the pH-activated and ion-translocating states J. Mol. Biol. 388 2009 659 672
    • (2009) J. Mol. Biol. , vol.388 , pp. 659-672
    • Appel, M.1    Hizlan, D.2    Vinothkumar, K.R.3    Ziegler, C.4    Kühlbrandt, W.5
  • 3
    • 33846505059 scopus 로고    scopus 로고
    • Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter
    • O. Boudker, R.M. Ryan, D. Yernool, K. Shimamoto, and E. Gouaux 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
  • 4
    • 77952854330 scopus 로고    scopus 로고
    • Cross-linking of trans reentrant loops in the Na(+)-citrate transporter CitS of Klebsiella pneumoniae
    • A. Dobrowolski, F. Fusetti, and J.S. Lolkema Cross-linking of trans reentrant loops in the Na(+)-citrate transporter CitS of Klebsiella pneumoniae Biochemistry 49 2010 4509 4515
    • (2010) Biochemistry , vol.49 , pp. 4509-4515
    • Dobrowolski, A.1    Fusetti, F.2    Lolkema, J.S.3
  • 5
    • 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
  • 6
    • 78650297251 scopus 로고    scopus 로고
    • The structural basis of secondary active transport mechanisms
    • L.R. Forrest, R. Krämer, and C. Ziegler The structural basis of secondary active transport mechanisms Biochim. Biophys. Acta 1807 2011 167 188
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 167-188
    • Forrest, L.R.1    Krämer, R.2    Ziegler, C.3
  • 7
    • 36049000626 scopus 로고    scopus 로고
    • 2dx-merge: Data management and merging for 2D crystal images
    • B. Gipson, X. Zeng, and H. Stahlberg 2dx-merge: data management and merging for 2D crystal images J. Struct. Biol. 160 2007 375 384
    • (2007) J. Struct. Biol. , vol.160 , pp. 375-384
    • Gipson, B.1    Zeng, X.2    Stahlberg, H.3
  • 9
    • 78751605214 scopus 로고    scopus 로고
    • Structure of the archaeal Na+/H+ antiporter NhaP1 and functional role of transmembrane helix 1
    • P. Goswami, C. Paulino, D. Hizlan, J. Vonck, O. Yildiz, and W. Kühlbrandt Structure of the archaeal Na+/H+ antiporter NhaP1 and functional role of transmembrane helix 1 EMBO J. 30 2011 439 449
    • (2011) EMBO J. , vol.30 , pp. 439-449
    • Goswami, P.1    Paulino, C.2    Hizlan, D.3    Vonck, J.4    Yildiz, O.5    Kühlbrandt, W.6
  • 10
    • 65249143983 scopus 로고    scopus 로고
    • Beta-sheet-dependent dimerization is essential for the stability of NhaA Na+/H+ antiporter
    • K. Herz, A. Rimon, G. Jeschke, and E. Padan Beta-sheet-dependent dimerization is essential for the stability of NhaA Na+/H+ antiporter J. Biol. Chem. 284 2009 6337 6347
    • (2009) J. Biol. Chem. , vol.284 , pp. 6337-6347
    • Herz, K.1    Rimon, A.2    Jeschke, G.3    Padan, E.4
  • 11
    • 21744436321 scopus 로고    scopus 로고
    • Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH
    • C. Hunte, E. Screpanti, M. Venturi, A. Rimon, E. Padan, and H. Michel 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
  • 12
    • 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
  • 13
    • 84858707945 scopus 로고    scopus 로고
    • Projection structure of the secondary citrate/sodium symporter CitS at 6 Å resolution by electron crystallography
    • F. Kebbel, M. Kurz, M.G. Grütter, and H. Stahlberg Projection structure of the secondary citrate/sodium symporter CitS at 6 Å resolution by electron crystallography J. Mol. Biol. 418 2012 117 126
    • (2012) J. Mol. Biol. , vol.418 , pp. 117-126
    • Kebbel, F.1    Kurz, M.2    Grütter, M.G.3    Stahlberg, H.4
  • 14
    • 66249098083 scopus 로고    scopus 로고
    • Unlocking the molecular secrets of sodium-coupled transporters
    • H. Krishnamurthy, C.L. Piscitelli, and E. Gouaux Unlocking the molecular secrets of sodium-coupled transporters Nature 459 2009 347 355
    • (2009) Nature , vol.459 , pp. 347-355
    • Krishnamurthy, H.1    Piscitelli, C.L.2    Gouaux, E.3
  • 15
    • 79960635001 scopus 로고    scopus 로고
    • Cross-linking of dimeric CitS and GltS transport proteins
    • T. Krupnik, A. Dobrowolski, and J.S. Lolkema Cross-linking of dimeric CitS and GltS transport proteins Mol. Membr. Biol. 28 2011 243 253
    • (2011) Mol. Membr. Biol. , vol.28 , pp. 243-253
    • Krupnik, T.1    Dobrowolski, A.2    Lolkema, J.S.3
  • 16
    • 35649017588 scopus 로고    scopus 로고
    • Kinetic evidence is consistent with the rocker-switch mechanism of membrane transport by GlpT
    • C.J. Law, Q. Yang, C. Soudant, P.C. Maloney, and D.N. Wang Kinetic evidence is consistent with the rocker-switch mechanism of membrane transport by GlpT Biochemistry 46 2007 12190 12197
    • (2007) Biochemistry , vol.46 , pp. 12190-12197
    • Law, C.J.1    Yang, Q.2    Soudant, C.3    Maloney, P.C.4    Wang, D.N.5
  • 17
    • 33751184200 scopus 로고    scopus 로고
    • Domain structure and pore loops in the 2-hydroxycarboxylate transporter family
    • J.S. Lolkema Domain structure and pore loops in the 2-hydroxycarboxylate transporter family J. Mol. Microbiol. Biotechnol. 11 2006 318 325
    • (2006) J. Mol. Microbiol. Biotechnol. , vol.11 , pp. 318-325
    • Lolkema, J.S.1
  • 18
    • 0031920140 scopus 로고    scopus 로고
    • Estimation of structural similarity of membrane proteins by hydropathy profile alignment
    • J.S. Lolkema, and D.J. Slotboom Estimation of structural similarity of membrane proteins by hydropathy profile alignment Mol. Membr. Biol. 15 1998 33 42
    • (1998) Mol. Membr. Biol. , vol.15 , pp. 33-42
    • Lolkema, J.S.1    Slotboom, D.J.2
  • 19
    • 0037432531 scopus 로고    scopus 로고
    • Classification of 29 families of secondary transport proteins into a single structural class using hydropathy profile analysis
    • J.S. Lolkema, and D.J. Slotboom Classification of 29 families of secondary transport proteins into a single structural class using hydropathy profile analysis J. Mol. Biol. 327 2003 901 909
    • (2003) J. Mol. Biol. , vol.327 , pp. 901-909
    • Lolkema, J.S.1    Slotboom, D.J.2
  • 20
    • 0028256431 scopus 로고
    • Transport of citrate catalyzed by the sodium-dependent citrate carrier of Klebsiella pneumoniae is obligatorily coupled to the transport of two sodium ions
    • J.S. Lolkema, H. Enequist, and M.E. van der Rest Transport of citrate catalyzed by the sodium-dependent citrate carrier of Klebsiella pneumoniae is obligatorily coupled to the transport of two sodium ions Eur. J. Biochem. 220 1994 469 475
    • (1994) Eur. J. Biochem. , vol.220 , pp. 469-475
    • Lolkema, J.S.1    Enequist, H.2    Van Der Rest, M.E.3
  • 21
    • 18444381459 scopus 로고    scopus 로고
    • Secondary transporters of the 2HCT family contain two homologous domains with inverted membrane topology and trans re-entrant loops
    • J.S. Lolkema, I. Sobczak, and D.J. Slotboom Secondary transporters of the 2HCT family contain two homologous domains with inverted membrane topology and trans re-entrant loops FEBS J. 272 2005 2334 2344
    • (2005) FEBS J. , vol.272 , pp. 2334-2344
    • Lolkema, J.S.1    Sobczak, I.2    Slotboom, D.J.3
  • 22
    • 84869884515 scopus 로고    scopus 로고
    • Structure and mechanism of a bacterial sodium-dependent dicarboxylate transporter
    • R. Mancusso, G.G. Gregorio, Q. Liu, and D.N. Wang Structure and mechanism of a bacterial sodium-dependent dicarboxylate transporter Nature 491 2012 622 626
    • (2012) Nature , vol.491 , pp. 622-626
    • Mancusso, R.1    Gregorio, G.G.2    Liu, Q.3    Wang, D.N.4
  • 23
    • 67650472373 scopus 로고    scopus 로고
    • Projection structure by single-particle electron microscopy of secondary transport proteins GltT, CitS, and GltS
    • K.B. Mościcka, T. Krupnik, E.J. Boekema, and J.S. Lolkema Projection structure by single-particle electron microscopy of secondary transport proteins GltT, CitS, and GltS Biochemistry 48 2009 6618 6623
    • (2009) Biochemistry , vol.48 , pp. 6618-6623
    • Mościcka, K.B.1    Krupnik, T.2    Boekema, E.J.3    Lolkema, J.S.4
  • 24
    • 79961025427 scopus 로고    scopus 로고
    • The role of trimerization in the osmoregulated betaine transporter BetP
    • C. Perez, K. Khafizov, L.R. Forrest, R. Krämer, and C. Ziegler The role of trimerization in the osmoregulated betaine transporter BetP EMBO Rep. 12 2011 804 810
    • (2011) EMBO Rep. , vol.12 , pp. 804-810
    • Perez, C.1    Khafizov, K.2    Forrest, L.R.3    Krämer, R.4    Ziegler, C.5
  • 26
    • 0030042331 scopus 로고    scopus 로고
    • Functional properties of the purified Na(+)-dependent citrate carrier of Klebsiella pneumoniae: Evidence for asymmetric orientation of the carrier protein in proteoliposomes
    • K.M. Pos, and P. Dimroth Functional properties of the purified Na(+)-dependent citrate carrier of Klebsiella pneumoniae: evidence for asymmetric orientation of the carrier protein in proteoliposomes Biochemistry 35 1996 1018 1026
    • (1996) Biochemistry , vol.35 , pp. 1018-1026
    • Pos, K.M.1    Dimroth, P.2
  • 27
    • 72449164409 scopus 로고    scopus 로고
    • Transport mechanism of a bacterial homologue of glutamate transporters
    • N. Reyes, C. Ginter, and O. Boudker Transport mechanism of a bacterial homologue of glutamate transporters Nature 462 2009 880 885
    • (2009) Nature , vol.462 , pp. 880-885
    • Reyes, N.1    Ginter, C.2    Boudker, O.3
  • 28
    • 0343603660 scopus 로고    scopus 로고
    • A functional-phylogenetic classification system for transmembrane solute transporters
    • M.H. Saier Jr. A functional-phylogenetic classification system for transmembrane solute transporters Microbiol. Mol. Biol. Rev. 64 2000 354 411
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 354-411
    • Saier, Jr.M.H.1
  • 30
    • 29144503678 scopus 로고    scopus 로고
    • The 2-hydroxycarboxylate transporter family: Physiology, structure, and mechanism
    • I. Sobczak, and J.S. Lolkema The 2-hydroxycarboxylate transporter family: physiology, structure, and mechanism Microbiol. Mol. Biol. Rev. 69 2005 665 695
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 665-695
    • Sobczak, I.1    Lolkema, J.S.2
  • 31
    • 16844370145 scopus 로고    scopus 로고
    • Loop VIII/IX of the Na+-citrate transporter CitS of Klebsiella pneumoniae folds into an amphipathic surface helix
    • I. Sobczak, and J.S. Lolkema Loop VIII/IX of the Na+-citrate transporter CitS of Klebsiella pneumoniae folds into an amphipathic surface helix Biochemistry 44 2005 5461 5470
    • (2005) Biochemistry , vol.44 , pp. 5461-5470
    • Sobczak, I.1    Lolkema, J.S.2
  • 32
    • 15744387867 scopus 로고    scopus 로고
    • Structural and mechanistic diversity of secondary transporters
    • I. Sobczak, and J.S. Lolkema Structural and mechanistic diversity of secondary transporters Curr. Opin. Microbiol. 8 2005 161 167
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 161-167
    • Sobczak, I.1    Lolkema, J.S.2
  • 33
    • 84867657593 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of glucose transporters GLUT1-4
    • L. Sun, X. Zeng, C. Yan, X. Sun, X. Gong, Y. Rao, and N. Yan Crystal structure of a bacterial homologue of glucose transporters GLUT1-4 Nature 490 2012 361 366
    • (2012) Nature , vol.490 , pp. 361-366
    • Sun, L.1    Zeng, X.2    Yan, C.3    Sun, X.4    Gong, X.5    Rao, Y.6    Yan, N.7
  • 34
    • 80055018057 scopus 로고    scopus 로고
    • Membrane topology screen of secondary transport proteins in structural class ST[3] of the MemGen classification. Confirmation and structural diversity
    • R. ter Horst, and J.S. Lolkema Membrane topology screen of secondary transport proteins in structural class ST[3] of the MemGen classification. Confirmation and structural diversity Biochim. Biophys. Acta 1818 2012 72 81
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 72-81
    • Ter Horst, R.1    Lolkema, J.S.2
  • 35
    • 77955984465 scopus 로고    scopus 로고
    • Coupling electron cryomicroscopy and X-ray crystallography to understand secondary active transport
    • C.J. Tsai, and C. Ziegler Coupling electron cryomicroscopy and X-ray crystallography to understand secondary active transport Curr. Opin. Struct. Biol. 20 2010 448 455
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 448-455
    • Tsai, C.J.1    Ziegler, C.2
  • 36
    • 0346874401 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer
    • I. Ubarretxena-Belandia, J.M. Baldwin, S. Schuldiner, and C.G. Tate Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer EMBO J. 22 2003 6175 6181
    • (2003) EMBO J. , vol.22 , pp. 6175-6181
    • Ubarretxena-Belandia, I.1    Baldwin, J.M.2    Schuldiner, S.3    Tate, C.G.4
  • 37
    • 0026636707 scopus 로고
    • Mechanism of Na(+)-dependent citrate transport in Klebsiella pneumoniae
    • M.E. van der Rest, D. Molenaar, and W.N. Konings Mechanism of Na(+)-dependent citrate transport in Klebsiella pneumoniae J. Bacteriol. 174 1992 4893 4898
    • (1992) J. Bacteriol. , vol.174 , pp. 4893-4898
    • Van Der Rest, M.E.1    Molenaar, D.2    Konings, W.N.3
  • 38
    • 0034213082 scopus 로고    scopus 로고
    • Membrane topology of the Na(+)/citrate transporter CitS of Klebsiella pneumoniae by insertion mutagenesis
    • M. van Geest, and J.S. Lolkema Membrane topology of the Na(+)/citrate transporter CitS of Klebsiella pneumoniae by insertion mutagenesis Biochim. Biophys. Acta 1466 2000 328 338
    • (2000) Biochim. Biophys. Acta , vol.1466 , pp. 328-338
    • Van Geest, M.1    Lolkema, J.S.2
  • 39
    • 24644470065 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of Na+/Cl-dependent neurotransmitter transporters
    • A. Yamashita, S.K. Singh, T. Kawate, Y. Jin, and E. Gouaux 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.