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Volumn 113, Issue 4, 2016, Pages 852-858

Enzymatic protein switches built from paralogous input domains

Author keywords

Biosensors; Periplasmic binding proteins; Protein engineering; Protein switches; Synthetic biology

Indexed keywords

BINS; BIOLOGY; BIOSENSORS;

EID: 84959519456     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.25852     Document Type: Article
Times cited : (23)

References (30)
  • 1
    • 0020069175 scopus 로고
    • Purification and properties of a periplasmic D-xylose-binding protein from Escherichia coli K-12
    • Ahlem C, Huisman W, Neslund G, Dahms AS. 1982. Purification and properties of a periplasmic D-xylose-binding protein from Escherichia coli K-12. J Biol Chem 257(6):2926-2931.
    • (1982) J Biol Chem , vol.257 , Issue.6 , pp. 2926-2931
    • Ahlem, C.1    Huisman, W.2    Neslund, G.3    Dahms, A.S.4
  • 2
    • 82555170281 scopus 로고    scopus 로고
    • Structure of the Escherichia coli phosphonate binding protein PhnD and rationally optimized phosphonate biosensors
    • Alicea I, Marvin JS, Miklos AE, Ellington AD, Looger LL, Schreiter ER. 2011. Structure of the Escherichia coli phosphonate binding protein PhnD and rationally optimized phosphonate biosensors. J Mol Biol 414:356-369.
    • (2011) J Mol Biol , vol.414 , pp. 356-369
    • Alicea, I.1    Marvin, J.S.2    Miklos, A.E.3    Ellington, A.D.4    Looger, L.L.5    Schreiter, E.R.6
  • 3
    • 84878323463 scopus 로고    scopus 로고
    • Non-allosteric enzyme switches possess larger effector-induced changes in thermodynamic stability than their non-switch analogs
    • Choi JH, San A, Ostermeier M. 2013. Non-allosteric enzyme switches possess larger effector-induced changes in thermodynamic stability than their non-switch analogs. Prot Sci 22:475-485.
    • (2013) Prot Sci , vol.22 , pp. 475-485
    • Choi, J.H.1    San, A.2    Ostermeier, M.3
  • 4
    • 84928799061 scopus 로고    scopus 로고
    • Design of protein switches based on an ensemble model of allostery
    • Choi JH, Laurent AH, Hilser VJ, Ostermeier M. 2015. Design of protein switches based on an ensemble model of allostery. Nat Commun 6:6968.
    • (2015) Nat Commun , vol.6 , pp. 6968
    • Choi, J.H.1    Laurent, A.H.2    Hilser, V.J.3    Ostermeier, M.4
  • 6
    • 33645297396 scopus 로고    scopus 로고
    • Binding of glucose to the D-galactose/D-glucose-binding protein from Escherichia coli restores the native protein secondary structure and thermostability that are lost upon calcium depletion
    • D'Auria S, Ausili A, Marabotti A, Varriale A, Scognamiglio B, Staiano M, Bertoli E, Rossi M, Tanfani F. 2006. Binding of glucose to the D-galactose/D-glucose-binding protein from Escherichia coli restores the native protein secondary structure and thermostability that are lost upon calcium depletion. J Biochem 139:213-221.
    • (2006) J Biochem , vol.139 , pp. 213-221
    • D'Auria, S.1    Ausili, A.2    Marabotti, A.3    Varriale, A.4    Scognamiglio, B.5    Staiano, M.6    Bertoli, E.7    Rossi, M.8    Tanfani, F.9
  • 8
    • 24344451972 scopus 로고    scopus 로고
    • Construction and optimization of a family of genetically encoded metabolite sensors by semirational protein engineering
    • Deuschle K, Okumuto S, Fehr M, Looger LL, Kozhukh L, Frommer WB. 2005. Construction and optimization of a family of genetically encoded metabolite sensors by semirational protein engineering. Prot Sci 14:2304-2314.
    • (2005) Prot Sci , vol.14 , pp. 2304-2314
    • Deuschle, K.1    Okumuto, S.2    Fehr, M.3    Looger, L.L.4    Kozhukh, L.5    Frommer, W.B.6
  • 9
    • 4143115810 scopus 로고    scopus 로고
    • Periplasmic binding proteins: A versatile superfamily for protein engineering
    • Dwyer MA, Hellinga HW. 2004. Periplasmic binding proteins: A versatile superfamily for protein engineering. Curr Opin Struct Biol 14(4):495-504.
    • (2004) Curr Opin Struct Biol , vol.14 , Issue.4 , pp. 495-504
    • Dwyer, M.A.1    Hellinga, H.W.2
  • 10
    • 8844263869 scopus 로고    scopus 로고
    • A molecular switch created by in vitro recombination of nonhomologous genes
    • Guntas G, Mitchell SF, Ostermeier M. 2004. A molecular switch created by in vitro recombination of nonhomologous genes. Chem Biol 11(11):1483-1487.
    • (2004) Chem Biol , vol.11 , Issue.11 , pp. 1483-1487
    • Guntas, G.1    Mitchell, S.F.2    Ostermeier, M.3
  • 11
    • 0346500466 scopus 로고    scopus 로고
    • Creation of an allosteric enzyme by domain insertion
    • Guntas G, Ostemeier M. 2004. Creation of an allosteric enzyme by domain insertion. J Mol Biol 336(1):263-273.
    • (2004) J Mol Biol , vol.336 , Issue.1 , pp. 263-273
    • Guntas, G.1    Ostemeier, M.2
  • 12
    • 23844465160 scopus 로고    scopus 로고
    • Directed evolution of protein switches and their application to the creation of ligand-binding proteins
    • Guntas G, Mansell TJ, Kim JR, Ostermeier M. 2005. Directed evolution of protein switches and their application to the creation of ligand-binding proteins. Proc Natl Acad Sci USA 102(32):11224-11229.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.32 , pp. 11224-11229
    • Guntas, G.1    Mansell, T.J.2    Kim, J.R.3    Ostermeier, M.4
  • 13
    • 80855139801 scopus 로고    scopus 로고
    • In vitro recombination of non-homologous genes can result in gene fusions that confer a switching phenotype to cells
    • Heins RA, Choi JH, Sohka T, Ostermeier M. 2011. In vitro recombination of non-homologous genes can result in gene fusions that confer a switching phenotype to cells. PLoS ONE 6:e27302.
    • (2011) PLoS ONE , vol.6 , pp. e27302
    • Heins, R.A.1    Choi, J.H.2    Sohka, T.3    Ostermeier, M.4
  • 14
    • 24344509845 scopus 로고    scopus 로고
    • The role of calcium in the conformational dynamics and thermal stability of the D-galactose/D-glucose-binding protein from Escherichia coli
    • Herman P, Vecer J, Barvik I, Jr, Scognamiglio V, Staiano M, de Champdoré M, Varriale A, Rossi M, D'Auria S. 2005. The role of calcium in the conformational dynamics and thermal stability of the D-galactose/D-glucose-binding protein from Escherichia coli. Proteins 61(1):184-195.
    • (2005) Proteins , vol.61 , Issue.1 , pp. 184-195
    • Herman, P.1    Vecer, J.2    Barvik, I.3    Scognamiglio, V.4    Staiano, M.5    de Champdoré, M.6    Varriale, A.7    Rossi, M.8    D'Auria, S.9
  • 16
    • 84959554853 scopus 로고    scopus 로고
    • Designed Ankyrin Repeat Protein (DARPin) based platform to study bio-molecular interactions and develop biosensors
    • Doctoral Dissertation, The Johns Hopkins University, Accession Number 3525099.
    • Kanwar M. 2011. Designed Ankyrin Repeat Protein (DARPin) based platform to study bio-molecular interactions and develop biosensors. Doctoral Dissertation, The Johns Hopkins University, 182 pages; Accession Number 3525099.
    • (2011) , pp. 182
    • Kanwar, M.1
  • 19
    • 4143085977 scopus 로고    scopus 로고
    • Cruciform DNA structure underlies the etiology for palindrome-mediated human chromosomal translocations
    • Kurahashi H, Inagaki H, Yamada K, Ohye T, Taniguchi M, Emanuel BS, Toda T. 2004. Cruciform DNA structure underlies the etiology for palindrome-mediated human chromosomal translocations. J Biol Chem 279(34):35377-35383.
    • (2004) J Biol Chem , vol.279 , Issue.34 , pp. 35377-35383
    • Kurahashi, H.1    Inagaki, H.2    Yamada, K.3    Ohye, T.4    Taniguchi, M.5    Emanuel, B.S.6    Toda, T.7
  • 20
    • 0019087696 scopus 로고
    • The inverted repeat as a recognizable structure feature in supercoiled DNA molecules
    • Lilley DM. 1980. The inverted repeat as a recognizable structure feature in supercoiled DNA molecules. Proc Natl Acad Sci USA 77(11):6468-6472.
    • (1980) Proc Natl Acad Sci USA , vol.77 , Issue.11 , pp. 6468-6472
    • Lilley, D.M.1
  • 21
    • 80053936867 scopus 로고    scopus 로고
    • A genetically encoded, high-signal-to-noise maltose sensor
    • Marvin JS, Schreiter ER, Echevarría IM, Looger LL. 2011. A genetically encoded, high-signal-to-noise maltose sensor. Proteins 79(11):3025-3036.
    • (2011) Proteins , vol.79 , Issue.11 , pp. 3025-3036
    • Marvin, J.S.1    Schreiter, E.R.2    Echevarría, I.M.3    Looger, L.L.4
  • 22
    • 0027050193 scopus 로고
    • Structural homology between rbs repressor and ribose binding protein implies functional similarity
    • Mauzy CA, Hermodson MA. 1992. Structural homology between rbs repressor and ribose binding protein implies functional similarity. Prot Sci 1(7):843-849.
    • (1992) Prot Sci , vol.1 , Issue.7 , pp. 843-849
    • Mauzy, C.A.1    Hermodson, M.A.2
  • 23
    • 0345102549 scopus 로고    scopus 로고
    • Conformational changes of ribose-binding protein and two related repressors are tailored to fit the functional need
    • Mowbray SL, Bjorkman AJ. 1999. Conformational changes of ribose-binding protein and two related repressors are tailored to fit the functional need. J Mol Biol 294(2):487-499.
    • (1999) J Mol Biol , vol.294 , Issue.2 , pp. 487-499
    • Mowbray, S.L.1    Bjorkman, A.J.2
  • 24
    • 0019350114 scopus 로고
    • Cruciform structures in supercoiled DNA
    • Panayotatos N, Wells RD. 1981. Cruciform structures in supercoiled DNA. Nature 289(5797):466-470.
    • (1981) Nature , vol.289 , Issue.5797 , pp. 466-470
    • Panayotatos, N.1    Wells, R.D.2
  • 27
    • 77956944744 scopus 로고    scopus 로고
    • Conformational changes and ligand recognition of Escherichia coli D-xylose binding protein revealed
    • Sooriyaarachchi S, Ubhayasekera W, Park C, Mowbray SL. 2010. Conformational changes and ligand recognition of Escherichia coli D-xylose binding protein revealed. J Mol Biol 402(4):657-668.
    • (2010) J Mol Biol , vol.402 , Issue.4 , pp. 657-668
    • Sooriyaarachchi, S.1    Ubhayasekera, W.2    Park, C.3    Mowbray, S.L.4
  • 28
    • 84927740260 scopus 로고    scopus 로고
    • A triple mutant in the Ω-loop of TEM-1 β-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis
    • Stojanoski V, Chow DC, Hu L, Sankaran B, Gilbert HF, Prasad BV, Palzkill T. 2015. A triple mutant in the Ω-loop of TEM-1 β-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis. J Biol Chem 290(16):10382-10394.
    • (2015) J Biol Chem , vol.290 , Issue.16 , pp. 10382-10394
    • Stojanoski, V.1    Chow, D.C.2    Hu, L.3    Sankaran, B.4    Gilbert, H.F.5    Prasad, B.V.6    Palzkill, T.7
  • 29
    • 80053052797 scopus 로고    scopus 로고
    • Protein Switches identified from diverse insertion libraries created using S1 nuclease digestion of supercoiled-form plasmid DNA
    • Tullman J, Guntas G, Dumont M, Ostermeier M. 2011. Protein Switches identified from diverse insertion libraries created using S1 nuclease digestion of supercoiled-form plasmid DNA. Biotechnol Bioeng 108(11):2535-2543.
    • (2011) Biotechnol Bioeng , vol.108 , Issue.11 , pp. 2535-2543
    • Tullman, J.1    Guntas, G.2    Dumont, M.3    Ostermeier, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.