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Volumn 72, Issue 2, 2008, Pages 140-146

A small subset of signal peptidase residues are perturbed by signal peptide binding

Author keywords

Membrane protein; NMR; Signal peptidase; Signal peptide; Substrate binding

Indexed keywords

ALKALINE PHOSPHATASE; ASPARTIC ACID; ESCHERICHIA COLI PROTEIN; GLUTAMIC ACID; GLUTAMINE; GLYCINE; ISOLEUCINE; LYSINE; MEMBRANE PROTEIN; METHIONINE; PROTEIN PRECURSOR; SERINE; SIGNAL PEPTIDASE; SIGNAL PEPTIDASE I; SIGNAL PEPTIDE; THREONINE; VALINE;

EID: 47949106667     PISSN: 17470277     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1747-0285.2008.00685.x     Document Type: Article
Times cited : (8)

References (20)
  • 1
    • 0021100176 scopus 로고
    • Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope
    • Wolfe P.B., Wickner W., Goodman J.M. (1983) Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope. J Biol Chem 258 : 12073 12080.
    • (1983) J Biol Chem , vol.258 , pp. 12073-12080
    • Wolfe, P.B.1    Wickner, W.2    Goodman, J.M.3
  • 2
    • 0027317361 scopus 로고
    • Three-dimensional model for the membrane domain of Escherichia coli leader peptidase based on disulfide mapping
    • Whitley P., Nilsson L., von Heijne G. (1993) Three-dimensional model for the membrane domain of Escherichia coli leader peptidase based on disulfide mapping. Biochemistry 32 : 8534 8539.
    • (1993) Biochemistry , vol.32 , pp. 8534-8539
    • Whitley, P.1    Nilsson, L.2    Von Heijne, G.3
  • 3
    • 0037088648 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase apoenzyme: Implications for signal peptide binding and the Ser-Lys dyad mechanism
    • Paetzel M., Dalbey R.E., Strynadka N.C. (2002) Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanism. J Biol Chem 277 : 9512 9519.
    • (2002) J Biol Chem , vol.277 , pp. 9512-9519
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.3
  • 4
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor
    • Paetzel M., Dalbey R.E., Strynadka N.C. (1998) Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor. Nature 396 : 186 190.
    • (1998) Nature , vol.396 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.3
  • 5
    • 33846985979 scopus 로고    scopus 로고
    • Altered -3 substrate specificity of Escherichia coli signal peptidase 1 mutants as revealed by screening a combinatorial peptide library
    • Ekici O.D., Karla A., Paetzel M., Lively M.O., Pei D., Dalbey R.E. (2007) Altered -3 substrate specificity of Escherichia coli signal peptidase 1 mutants as revealed by screening a combinatorial peptide library. J Biol Chem 282 : 417 425.
    • (2007) J Biol Chem , vol.282 , pp. 417-425
    • Ekici, O.D.1    Karla, A.2    Paetzel, M.3    Lively, M.O.4    Pei, D.5    Dalbey, R.E.6
  • 6
    • 0034616343 scopus 로고    scopus 로고
    • Signal peptide determinants of SecA binding and stimulation of ATPase activity
    • Wang L., Miller A., Kendall D.A. (2000) Signal peptide determinants of SecA binding and stimulation of ATPase activity. J Biol Chem 275 : 10154 10159.
    • (2000) J Biol Chem , vol.275 , pp. 10154-10159
    • Wang, L.1    Miller, A.2    Kendall, D.A.3
  • 7
    • 0029147016 scopus 로고
    • Physical and conformational properties of synthetic idealized signal sequences parallel their biological function
    • Izard J.W., Doughty M.B., Kendall D.A. (1995) Physical and conformational properties of synthetic idealized signal sequences parallel their biological function. Biochemistry 34 : 9904 9912.
    • (1995) Biochemistry , vol.34 , pp. 9904-9912
    • Izard, J.W.1    Doughty, M.B.2    Kendall, D.A.3
  • 8
  • 9
  • 10
    • 0035104092 scopus 로고    scopus 로고
    • TM Finder: A prediction program for transmembrane protein segments using a combination of hydrophobicity and nonpolar phase helicity scales
    • Deber C.M., Wang C., Liu L.P., Prior A.S., Agrawal S., Muskat B.L., Cuticchia A.J. (2001) TM Finder: a prediction program for transmembrane protein segments using a combination of hydrophobicity and nonpolar phase helicity scales. Protein Sci 10 : 212 219.
    • (2001) Protein Sci , vol.10 , pp. 212-219
    • Deber, C.M.1    Wang, C.2    Liu, L.P.3    Prior, A.S.4    Agrawal, S.5    Muskat, B.L.6    Cuticchia, A.J.7
  • 11
    • 0031926765 scopus 로고    scopus 로고
    • Guidelines for membrane protein engineering derived from de novo designed model peptides
    • Liu L.P., Deber C.M. (1998) Guidelines for membrane protein engineering derived from de novo designed model peptides. Biopolymers 47 : 41 62.
    • (1998) Biopolymers , vol.47 , pp. 41-62
    • Liu, L.P.1    Deber, C.M.2
  • 13
    • 1942531294 scopus 로고    scopus 로고
    • Aqueous solubility and membrane interactions of hydrophobic peptides with peptoid tags
    • Tang Y.C., Deber C.M. (2004) Aqueous solubility and membrane interactions of hydrophobic peptides with peptoid tags. Biopolymers 76 : 110 118.
    • (2004) Biopolymers , vol.76 , pp. 110-118
    • Tang, Y.C.1    Deber, C.M.2
  • 14
    • 0028942966 scopus 로고
    • Characterization of a soluble, catalytically active form of Escherichia coli leader peptidase: Requirement of detergent or phospholipid for optimal activity
    • Tschantz W.R., Paetzel M., Cao G., Suciu D., Inouye M., Dalbey R.E. (1995) Characterization of a soluble, catalytically active form of Escherichia coli leader peptidase: requirement of detergent or phospholipid for optimal activity. Biochemistry 34 : 3935 3941.
    • (1995) Biochemistry , vol.34 , pp. 3935-3941
    • Tschantz, W.R.1    Paetzel, M.2    Cao, G.3    Suciu, D.4    Inouye, M.5    Dalbey, R.E.6
  • 15
    • 0030708525 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins
    • Hajduk P.J., Meadows R.P., Fesik S.W. (1997) Discovering high-affinity ligands for proteins. Science 278 : 497 499.
    • (1997) Science , vol.278 , pp. 497-499
    • Hajduk, P.J.1    Meadows, R.P.2    Fesik, S.W.3
  • 16
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker S.B., Hajduk P.J., Meadows R.P., Fesik S.W. (1996) Discovering high-affinity ligands for proteins: SAR by NMR. Science 274 : 1531 1534.
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 17
    • 0027733662 scopus 로고
    • A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidase
    • Tschantz W.R., Sung M., Delgado-Partin V.M., Dalbey R.E. (1993) A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidase. J Biol Chem 268 : 27349 27354.
    • (1993) J Biol Chem , vol.268 , pp. 27349-27354
    • Tschantz, W.R.1    Sung, M.2    Delgado-Partin, V.M.3    Dalbey, R.E.4
  • 18
    • 0034691249 scopus 로고    scopus 로고
    • Mutational evidence of transition state stabilization by serine 88 in Escherichia coli type I signal peptidase
    • Carlos J.L., Klenotic P.A., Paetzel M., Strynadka N.C., Dalbey R.E. (2000) Mutational evidence of transition state stabilization by serine 88 in Escherichia coli type I signal peptidase. Biochemistry 39 : 7276 7283.
    • (2000) Biochemistry , vol.39 , pp. 7276-7283
    • Carlos, J.L.1    Klenotic, P.A.2    Paetzel, M.3    Strynadka, N.C.4    Dalbey, R.E.5
  • 19
    • 14844332027 scopus 로고    scopus 로고
    • The identification of residues that control signal peptidase cleavage fidelity and substrate specificity
    • Karla A., Lively M.O., Paetzel M., Dalbey R. (2005) The identification of residues that control signal peptidase cleavage fidelity and substrate specificity. J Biol Chem 280 : 6731 6741.
    • (2005) J Biol Chem , vol.280 , pp. 6731-6741
    • Karla, A.1    Lively, M.O.2    Paetzel, M.3    Dalbey, R.4
  • 20
    • 0023052465 scopus 로고
    • Hydration and the lamellar to hexagonal II phase transition of phosphatidylethanolamine
    • Yeagle P.L., Sen A. (1986) Hydration and the lamellar to hexagonal II phase transition of phosphatidylethanolamine. Biochemistry 25 : 7518 7522.
    • (1986) Biochemistry , vol.25 , pp. 7518-7522
    • Yeagle, P.L.1    Sen, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.