메뉴 건너뛰기




Volumn 183, Issue 1, 2013, Pages 99-104

An arm-swapped dimer of the Streptococcus pyogenes pilin specific assembly factor SipA

Author keywords

LepA; Pilus assembly; Signal peptidase; SipA; Streptococcus pyogenes

Indexed keywords

BACTERIAL PROTEIN; DIMER; MONOMER; PILIN; PROTEIN SIPA; SIGNAL PEPTIDASE I; UNCLASSIFIED DRUG;

EID: 84879886240     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2013.05.021     Document Type: Article
Times cited : (6)

References (33)
  • 2
    • 57649181724 scopus 로고    scopus 로고
    • Modeling Escherichia coli signal peptidase complex with bound substrate: determinants in the mature peptide influencing signal peptide cleavage
    • Choo K.H., Tong J.C., Ranganathan S. Modeling Escherichia coli signal peptidase complex with bound substrate: determinants in the mature peptide influencing signal peptide cleavage. BMC Bioinf. 2008, 9(Suppl. 1):S15.
    • (2008) BMC Bioinf. , vol.9 , Issue.SUPPL. 1
    • Choo, K.H.1    Tong, J.C.2    Ranganathan, S.3
  • 3
    • 0032872798 scopus 로고    scopus 로고
    • Density modification for macromolecular phase improvement
    • Cowtan K.D., Zhang K.Y.J. Density modification for macromolecular phase improvement. Prog. Biophys. Mol. Bio. 1999, 72:245-270.
    • (1999) Prog. Biophys. Mol. Bio. , vol.72 , pp. 245-270
    • Cowtan, K.D.1    Zhang, K.Y.J.2
  • 4
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham M.W. Pathogenesis of group A streptococcal infections. Clin. Microbiol. Rev. 2000, 13:470-511.
    • (2000) Clin. Microbiol. Rev. , vol.13 , pp. 470-511
    • Cunningham, M.W.1
  • 5
    • 0022400507 scopus 로고
    • Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane
    • Dalbey R.E., Wickner W. Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane. J. Biol. Chem. 1985, 260:15925-15931.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15925-15931
    • Dalbey, R.E.1    Wickner, W.2
  • 6
    • 0030998468 scopus 로고    scopus 로고
    • The chemistry and enzymology of the type I signal peptidases
    • Dalbey R.E., Lively M.O., Bron S., van Dijl J.M. The chemistry and enzymology of the type I signal peptidases. Protein Sci. 1997, 6:1129-1138.
    • (1997) Protein Sci. , vol.6 , pp. 1129-1138
    • Dalbey, R.E.1    Lively, M.O.2    Bron, S.3    van Dijl, J.M.4
  • 10
    • 79951816315 scopus 로고    scopus 로고
    • Architects at the bacterial surface - sortases and the assembly of pili with isopeptide bonds
    • Hendrickx A.P., Budzik J.M., Oh S.Y., Schneewind O. Architects at the bacterial surface - sortases and the assembly of pili with isopeptide bonds. Nat. Rev. Microbiol. 2011, 9:166-176.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 166-176
    • Hendrickx, A.P.1    Budzik, J.M.2    Oh, S.Y.3    Schneewind, O.4
  • 11
    • 0024526131 scopus 로고
    • Conditionally lethal amber mutations in the leader peptidase gene of Escherichia coli
    • Inada T., Court D.L., Ito K., Nakamura Y. Conditionally lethal amber mutations in the leader peptidase gene of Escherichia coli. J. Bacteriol. 1989, 171:585-587.
    • (1989) J. Bacteriol. , vol.171 , pp. 585-587
    • Inada, T.1    Court, D.L.2    Ito, K.3    Nakamura, Y.4
  • 12
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 1993, 26:795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 13
    • 36849072428 scopus 로고    scopus 로고
    • Stabilizing isopeptide bonds revealed in gram-positive bacterial pilus structure
    • Kang H.J., Coulibaly F., Clow F., Proft T., Baker E.N. Stabilizing isopeptide bonds revealed in gram-positive bacterial pilus structure. Science 2007, 318:1625-1628.
    • (2007) Science , vol.318 , pp. 1625-1628
    • Kang, H.J.1    Coulibaly, F.2    Clow, F.3    Proft, T.4    Baker, E.N.5
  • 14
  • 21
    • 33646794930 scopus 로고    scopus 로고
    • A simple clustering algorithm can be accurate enough for use in calculations of pKs in macromolecules
    • Myers J., Grothaus G., Narayanan S., Onufriev A. A simple clustering algorithm can be accurate enough for use in calculations of pKs in macromolecules. Proteins 2006, 63:928-938.
    • (2006) Proteins , vol.63 , pp. 928-938
    • Myers, J.1    Grothaus, G.2    Narayanan, S.3    Onufriev, A.4
  • 23
    • 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. Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor. Nature 1998, 396:186-190.
    • (1998) Nature , vol.396 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.3
  • 24
    • 0033866745 scopus 로고    scopus 로고
    • The structure and mechanism of bacterial type I signal peptidases: A novel antibiotic target
    • Paetzel M., Dalbey R.E., Strynadka N.C.J. The structure and mechanism of bacterial type I signal peptidases: A novel antibiotic target. Pharmacol. Therapeut. 2000, 87:27-49.
    • (2000) Pharmacol. Therapeut. , vol.87 , pp. 27-49
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.J.3
  • 25
    • 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. Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanism. J. Biol. Chem. 2002, 277:9512-9519.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9512-9519
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.3
  • 26
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 1999, 6:458-463.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 28
    • 66249126841 scopus 로고    scopus 로고
    • Enzymatic investigation of the Staphylococcus aureus type I signal peptidase SpsB - implications for the search for novel antibiotics
    • Rao S.C.V., Bockstael K., Nath S., Engelborghs Y., Anne J., Geukens N. Enzymatic investigation of the Staphylococcus aureus type I signal peptidase SpsB - implications for the search for novel antibiotics. FEBS J. 2009, 276:3222-3234.
    • (2009) FEBS J. , vol.276 , pp. 3222-3234
    • Rao, S.C.V.1    Bockstael, K.2    Nath, S.3    Engelborghs, Y.4    Anne, J.5    Geukens, N.6
  • 29
    • 0002272684 scopus 로고    scopus 로고
    • SHELX applications to macromolecules
    • Sheldrick G.M. SHELX applications to macromolecules. NATO Adv. Sci. IC-Mat. 1998, 507:401-411.
    • (1998) NATO Adv. Sci. IC-Mat. , vol.507 , pp. 401-411
    • Sheldrick, G.M.1
  • 31
    • 0033818558 scopus 로고    scopus 로고
    • A truncated soluble Bacillus signal peptidase produced in Escherichia coli is subject to self-cleavage at its active site
    • van Roosmalen M.L., Jongbloed J.D.H., Kuipers A., Venema G., Bron S., van Dijl J.M. A truncated soluble Bacillus signal peptidase produced in Escherichia coli is subject to self-cleavage at its active site. J. Bacteriol. 2000, 182:5765-5770.
    • (2000) J. Bacteriol. , vol.182 , pp. 5765-5770
    • van Roosmalen, M.L.1    Jongbloed, J.D.H.2    Kuipers, A.3    Venema, G.4    Bron, S.5    van Dijl, J.M.6
  • 32
    • 38749129192 scopus 로고    scopus 로고
    • SipA is required for pilus formation in Streptococcus pyogenes serotype M3
    • Zahner D., Scott J.R. SipA is required for pilus formation in Streptococcus pyogenes serotype M3. J. Bacteriol. 2008, 190:527-535.
    • (2008) J. Bacteriol. , vol.190 , pp. 527-535
    • Zahner, D.1    Scott, J.R.2
  • 33
    • 0036037289 scopus 로고    scopus 로고
    • In vitro and in vivo self-cleavage of Streptococcus pneumoniae signal peptidase I
    • Zheng F., Angleton E.L., Lu J., Peng S.B. In vitro and in vivo self-cleavage of Streptococcus pneumoniae signal peptidase I. Eur. J. Biochem. 2002, 269:3969-3977.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3969-3977
    • Zheng, F.1    Angleton, E.L.2    Lu, J.3    Peng, S.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.