메뉴 건너뛰기




Volumn 82, Issue 2, 2014, Pages 336-346

Evolutionary relationship between 5+5 and 7+7 inverted repeat folds within the amino acid-polyamine-organocation superfamily

Author keywords

AdiC; UraA; Amino acid polyamine organocation; APC; Duplication; Hairpin; Superfamily

Indexed keywords

AMINO ACID POLYAMINE ORGANOCATION PROTEIN; CARRIER PROTEIN; UNCLASSIFIED DRUG;

EID: 84892679519     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24401     Document Type: Article
Times cited : (36)

References (39)
  • 1
    • 78650297251 scopus 로고    scopus 로고
    • The structural basis of secondary active transport mechanisms
    • Forrest LR, Kramer R, Ziegler C. The structural basis of secondary active transport mechanisms. Biochim Biophys Acta 2011;1807:167-188.
    • (2011) Biochim Biophys Acta , vol.1807 , pp. 167-188
    • Forrest, L.R.1    Kramer, R.2    Ziegler, C.3
  • 2
    • 0033886560 scopus 로고    scopus 로고
    • Families of transmembrane transporters selective for amino acids and their derivatives
    • Saier MH, Jr. Families of transmembrane transporters selective for amino acids and their derivatives. Microbiology 2000;146 (Part 8):1775-1795.
    • (2000) Microbiology , vol.146 , Issue.PART 8 , pp. 1775-1795
    • Saier Jr, M.H.1
  • 3
    • 73949083478 scopus 로고    scopus 로고
    • The rocking bundle: a mechanism for ion-coupled solute flux by symmetrical transporters
    • Forrest LR, Rudnick G. The rocking bundle: a mechanism for ion-coupled solute flux by symmetrical transporters. Physiology (Bethesda) 2009;24:377-386.
    • (2009) Physiology (Bethesda) , vol.24 , pp. 377-386
    • Forrest, L.R.1    Rudnick, G.2
  • 6
    • 0033886562 scopus 로고    scopus 로고
    • The amino acid/polyamine/organocation (APC) superfamily of transporters specific for amino acids, polyamines and organocations
    • Jack DL, Paulsen IT, Saier MH. The amino acid/polyamine/organocation (APC) superfamily of transporters specific for amino acids, polyamines and organocations. Microbiology 2000;146 (Part 8):1797-1814.
    • (2000) Microbiology , vol.146 , Issue.PART 8 , pp. 1797-1814
    • Jack, D.L.1    Paulsen, I.T.2    Saier, M.H.3
  • 8
    • 69249116947 scopus 로고    scopus 로고
    • Structure and mechanism of a Na+-independent amino acid transporter
    • Shaffer PL, Goehring A, Shankaranarayanan A, Gouaux E. Structure and mechanism of a Na+-independent amino acid transporter. Science 2009;325:1010-1014.
    • (2009) Science , vol.325 , pp. 1010-1014
    • Shaffer, P.L.1    Goehring, A.2    Shankaranarayanan, A.3    Gouaux, E.4
  • 9
    • 34548178234 scopus 로고    scopus 로고
    • Antidepressant binding site in a bacterial homologue of neurotransmitter transporters
    • Singh SK, Yamashita A, Gouaux E. Antidepressant binding site in a bacterial homologue of neurotransmitter transporters. Nature 2007;448:952-956.
    • (2007) Nature , vol.448 , pp. 952-956
    • Singh, S.K.1    Yamashita, A.2    Gouaux, E.3
  • 11
    • 84867092080 scopus 로고    scopus 로고
    • Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP
    • Perez C, Koshy C, Yildiz O, Ziegler C. Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP. Nature 2012;490:126-130.
    • (2012) Nature , vol.490 , pp. 126-130
    • Perez, C.1    Koshy, C.2    Yildiz, O.3    Ziegler, C.4
  • 15
    • 67849130558 scopus 로고    scopus 로고
    • TOPCONS: consensus prediction of membrane protein topology
    • (Web Server issue)
    • Bernsel A, Viklund H, Hennerdal A, Elofsson A. TOPCONS: consensus prediction of membrane protein topology. Nucleic Acids Res 2009;37(Web Server issue):W465-W468.
    • (2009) Nucleic Acids Res , vol.37
    • Bernsel, A.1    Viklund, H.2    Hennerdal, A.3    Elofsson, A.4
  • 16
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 2004;60(Part 12, Part 1):2256-2268.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 PART 1 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 17
    • 78650397484 scopus 로고    scopus 로고
    • A study of the evolution of inverted-topology repeats from LeuT-fold transporters using AlignMe
    • Khafizov K, Staritzbichler R, Stamm M, Forrest LR. A study of the evolution of inverted-topology repeats from LeuT-fold transporters using AlignMe. Biochemistry 2010;49:10702-10713.
    • (2010) Biochemistry , vol.49 , pp. 10702-10713
    • Khafizov, K.1    Staritzbichler, R.2    Stamm, M.3    Forrest, L.R.4
  • 18
    • 34447637751 scopus 로고    scopus 로고
    • Discontinuous membrane helices in transport proteins and their correlation with function
    • Screpanti E, Hunte C. Discontinuous membrane helices in transport proteins and their correlation with function. J Struct Biol 2007;159:261-267.
    • (2007) J Struct Biol , vol.159 , pp. 261-267
    • Screpanti, E.1    Hunte, C.2
  • 19
    • 84881647372 scopus 로고    scopus 로고
    • Mechanistic aspects of sodium-binding sites in LeuT-like fold symporters
    • Perez C, Ziegler C. Mechanistic aspects of sodium-binding sites in LeuT-like fold symporters. Biol Chem 2013;394:641-648.
    • (2013) Biol Chem , vol.394 , pp. 641-648
    • Perez, C.1    Ziegler, C.2
  • 20
    • 24644470065 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of Na+/Cl-dependent neurotransmitter transporters
    • Yamashita A, Singh SK, Kawate T, Jin Y, Gouaux E. Crystal structure of a bacterial homologue of Na+/Cl-dependent neurotransmitter transporters. Nature 2005;437:215-223.
    • (2005) Nature , vol.437 , pp. 215-223
    • Yamashita, A.1    Singh, S.K.2    Kawate, T.3    Jin, Y.4    Gouaux, E.5
  • 21
    • 79961025427 scopus 로고    scopus 로고
    • The role of trimerization in the osmoregulated betaine transporter BetP
    • Perez C, Khafizov K, Forrest LR, Kramer R, Ziegler C. The role of trimerization in the osmoregulated betaine transporter BetP. EMBO Rep 2011;12:804-810.
    • (2011) EMBO Rep , vol.12 , pp. 804-810
    • Perez, C.1    Khafizov, K.2    Forrest, L.R.3    Kramer, R.4    Ziegler, C.5
  • 24
    • 84855902765 scopus 로고    scopus 로고
    • Anion transport by the cochlear motor protein prestin
    • Schanzler M, Fahlke C. Anion transport by the cochlear motor protein prestin. J Physiol 2012;590 (Part 2):259-272.
    • (2012) J Physiol , vol.590 , Issue.PART 2 , pp. 259-272
    • Schanzler, M.1    Fahlke, C.2
  • 25
    • 84861185139 scopus 로고    scopus 로고
    • BioV Suite-a collection of programs for the study of transport protein evolution
    • Reddy VS, Saier MH, Jr. BioV Suite-a collection of programs for the study of transport protein evolution. FEBS J 2012;279:2036-2046.
    • (2012) FEBS J , vol.279 , pp. 2036-2046
    • Reddy, V.S.1    Saier Jr, M.H.2
  • 26
    • 84883594897 scopus 로고    scopus 로고
    • Memoir: template-based structure prediction for membrane proteins
    • 2013;41 (Web Server issue):W379-W383
    • Ebejer JP, Hill JR, Kelm S, Shi J, Deane CM. Memoir: template-based structure prediction for membrane proteins. Nucleic Acids Res 2013;41 (Web Server issue):W379-W383.
    • Nucleic Acids Res
    • Ebejer, J.P.1    Hill, J.R.2    Kelm, S.3    Shi, J.4    Deane, C.M.5
  • 27
    • 84856771753 scopus 로고    scopus 로고
    • Camps 2.0: exploring the sequence and structure space of prokaryotic, eukaryotic, and viral membrane proteins
    • Neumann S, Hartmann H, Martin-Galiano AJ, Fuchs A, Frishman D. Camps 2.0: exploring the sequence and structure space of prokaryotic, eukaryotic, and viral membrane proteins. Proteins 2012;80:839-857.
    • (2012) Proteins , vol.80 , pp. 839-857
    • Neumann, S.1    Hartmann, H.2    Martin-Galiano, A.J.3    Fuchs, A.4    Frishman, D.5
  • 28
    • 84867547605 scopus 로고    scopus 로고
    • Insights to the evolution of nucleobase-ascorbate transporters (NAT/NCS2 family) from the Cys-scanning analysis of xanthine permease XanQ
    • Frillingos S. Insights to the evolution of nucleobase-ascorbate transporters (NAT/NCS2 family) from the Cys-scanning analysis of xanthine permease XanQ. Int J Biochem Mol Biol 2012;3:250-272.
    • (2012) Int J Biochem Mol Biol , vol.3 , pp. 250-272
    • Frillingos, S.1
  • 29
    • 84864353522 scopus 로고    scopus 로고
    • Identification of the substrate recognition and transport pathway in a eukaryotic member of the nucleobase-ascorbate transporter (NAT) family
    • Kosti V, Lambrinidis G, Myrianthopoulos V, Diallinas G, Mikros E. Identification of the substrate recognition and transport pathway in a eukaryotic member of the nucleobase-ascorbate transporter (NAT) family. PLoS One 2012;7:e41939.
    • (2012) PLoS One , vol.7
    • Kosti, V.1    Lambrinidis, G.2    Myrianthopoulos, V.3    Diallinas, G.4    Mikros, E.5
  • 30
    • 84860862465 scopus 로고    scopus 로고
    • Substrate selectivity of YgfU, a uric acid transporter from Escherichia coli
    • Papakostas K, Frillingos S. Substrate selectivity of YgfU, a uric acid transporter from Escherichia coli. J Biol Chem 2012;287:15684-15695.
    • (2012) J Biol Chem , vol.287 , pp. 15684-15695
    • Papakostas, K.1    Frillingos, S.2
  • 31
    • 80655144745 scopus 로고    scopus 로고
    • The role of transmembrane segment TM3 in the xanthine permease XanQ of Escherichia coli
    • Karena E, Frillingos S. The role of transmembrane segment TM3 in the xanthine permease XanQ of Escherichia coli. J Biol Chem 2011;286:39595-39605.
    • (2011) J Biol Chem , vol.286 , pp. 39595-39605
    • Karena, E.1    Frillingos, S.2
  • 32
    • 0034824349 scopus 로고    scopus 로고
    • The drug/metabolite transporter superfamily
    • Jack DL, Yang NM, Saier MH, Jr. The drug/metabolite transporter superfamily. Eur J Biochem 2001;268:3620-3639.
    • (2001) Eur J Biochem , vol.268 , pp. 3620-3639
    • Jack, D.L.1    Yang, N.M.2    Saier Jr, M.H.3
  • 34
    • 84877303485 scopus 로고    scopus 로고
    • A comparative study of structures and structural transitions of secondary transporters with the LeuT fold
    • Jeschke G. A comparative study of structures and structural transitions of secondary transporters with the LeuT fold. Eur Biophys J 2013;42:181-197.
    • (2013) Eur Biophys J , vol.42 , pp. 181-197
    • Jeschke, G.1
  • 35
    • 84870215353 scopus 로고    scopus 로고
    • Amino acid secondary transporters: toward a common transport mechanism
    • Schweikhard ES, Ziegler CM. Amino acid secondary transporters: toward a common transport mechanism. Curr Top Membr 2012;70:1-28.
    • (2012) Curr Top Membr , vol.70 , pp. 1-28
    • Schweikhard, E.S.1    Ziegler, C.M.2
  • 36
    • 44349103701 scopus 로고    scopus 로고
    • Solute carrier 11 cation symport requires distinct residues in transmembrane helices 1 and 6
    • Courville P, Urbankova E, Rensing C, Chaloupka R, Quick M, Cellier MF. Solute carrier 11 cation symport requires distinct residues in transmembrane helices 1 and 6. J Biol Chem 2008;283:9651-9658.
    • (2008) J Biol Chem , vol.283 , pp. 9651-9658
    • Courville, P.1    Urbankova, E.2    Rensing, C.3    Chaloupka, R.4    Quick, M.5    Cellier, M.F.6
  • 37
    • 0035783063 scopus 로고    scopus 로고
    • Fold change in evolution of protein structures
    • Grishin NV. Fold change in evolution of protein structures. J Struct Biol 2001;134:167-185.
    • (2001) J Struct Biol , vol.134 , pp. 167-185
    • Grishin, N.V.1
  • 38
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Soding J. Protein homology detection by HMM-HMM comparison. Bioinformatics 2005;21:951-960.
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Soding, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.