메뉴 건너뛰기




Volumn 79, Issue 9, 2011, Pages 2764-2769

A novel "open-form" structure of sortaseC from Streptococcus suis

Author keywords

Class C sortase; Helical conformation; Protein structure; SortaseC specific lid; Substrate binding site

Indexed keywords

SORTASE; SORTASE C; UNCLASSIFIED DRUG;

EID: 80051574122     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.23093     Document Type: Note
Times cited : (14)

References (23)
  • 1
    • 0842281609 scopus 로고    scopus 로고
    • The biology of Gram-positive sortase enzymes
    • Paterson GK, Mitchell TJ. The biology of Gram-positive sortase enzymes. Trends Microbiol 2004; 12: 89-95.
    • (2004) Trends Microbiol , vol.12 , pp. 89-95
    • Paterson, G.K.1    Mitchell, T.J.2
  • 2
    • 33645137247 scopus 로고    scopus 로고
    • Sortases and the art of anchoring proteins to the envelopes of Gram-positive bacteria
    • Marraffini LA, Dedent AC, Schneewind O. Sortases and the art of anchoring proteins to the envelopes of Gram-positive bacteria. Microbiol Mol Biol Rev 2006; 70: 192-221.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 192-221
    • Marraffini, L.A.1    Dedent, A.C.2    Schneewind, O.3
  • 3
    • 16844372650 scopus 로고    scopus 로고
    • Sorting sortases: a nomenclature proposal for the various sortases of Gram-positive bacteria
    • Dramsi S, Trieu-Cuot P, Bierne H. Sorting sortases: a nomenclature proposal for the various sortases of Gram-positive bacteria. Res Microbiol 2005; 156: 289-297.
    • (2005) Res Microbiol , vol.156 , pp. 289-297
    • Dramsi, S.1    Trieu-Cuot, P.2    Bierne, H.3
  • 4
    • 0345689425 scopus 로고    scopus 로고
    • Assembly of pili on the surface of Corynebacterium diphtheriae
    • Ton-That H, Schneewind O. Assembly of pili on the surface of Corynebacterium diphtheriae. Mol Microbiol 2003; 50: 1429-1438.
    • (2003) Mol Microbiol , vol.50 , pp. 1429-1438
    • Ton-That, H.1    Schneewind, O.2
  • 9
    • 3543073805 scopus 로고    scopus 로고
    • Crystal structures of Staphylococcus aureus sortase A and its substrate complex
    • Zong Y, Bice TW, Ton-That H, Schneewind O, Narayana SV. Crystal structures of Staphylococcus aureus sortase A and its substrate complex. J Biol Chem 2004; 279: 31383-31389.
    • (2004) J Biol Chem , vol.279 , pp. 31383-31389
    • Zong, Y.1    Bice, T.W.2    Ton-That, H.3    Schneewind, O.4    Narayana, S.V.5
  • 10
    • 3142649047 scopus 로고    scopus 로고
    • Structures of sortase B from Staphylococcus aureus and Bacillus anthracis reveal catalytic amino acid triad in the active site
    • Zhang R, Wu R, Joachimiak G, Mazmanian SK, Missiakas DM, Gornicki P, Schneewind O, Joachimiak A. Structures of sortase B from Staphylococcus aureus and Bacillus anthracis reveal catalytic amino acid triad in the active site. Structure 2004; 12: 1147-1156.
    • (2004) Structure , vol.12 , pp. 1147-1156
    • Zhang, R.1    Wu, R.2    Joachimiak, G.3    Mazmanian, S.K.4    Missiakas, D.M.5    Gornicki, P.6    Schneewind, O.7    Joachimiak, A.8
  • 13
    • 70449442758 scopus 로고    scopus 로고
    • Sortase activity is controlled by a flexible lid in the pilus biogenesis mechanism of Gram-positive pathogens
    • Manzano C, Izore T, Job V, Di Guilmi AM, Dessen A. Sortase activity is controlled by a flexible lid in the pilus biogenesis mechanism of Gram-positive pathogens. Biochemistry 2009; 48: 10549-10557.
    • (2009) Biochemistry , vol.48 , pp. 10549-10557
    • Manzano, C.1    Izore, T.2    Job, V.3    Di Guilmi, A.M.4    Dessen, A.5
  • 17
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray Diffraction Data Collected in Oscillation Mode, Methods in Enzymology
    • C.W. Carter, Jr., amp; R. M. Sweet, Eds., New York: Academic Press 276.
    • Otwinowski Z, Minor W. Processing of X-ray Diffraction Data Collected in Oscillation Mode, Methods in Enzymology, Volume 276: Macromolecular Crystallography, part A, C.W. Carter, Jr., & R. M. Sweet, Eds., New York: Academic Press 1997;276: 307-326.
    • (1997) Macromolecular Crystallography, part A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 19
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger TC. Maximum-likelihood density modification. Acta Crystallogr D Biol Crystallogr 2000; 56 (Part 8): 965-972.
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , Issue.PART 8 , pp. 965-972
    • Terwilliger, T.C.1
  • 20
    • 0028103275 scopus 로고
    • Collaborative Computing Project Number 4. The CCP4 suite: programs for protein crystallography
    • Collaborative Computing Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994; 50 (Part 5): 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , Issue.PART 5 , pp. 760-763
  • 21
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 2004; 60 (Part 12 Part 1): 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 22
  • 23
    • 79952260321 scopus 로고    scopus 로고
    • Structure of the sortase AcSrtC-1 from Actinomyces oris
    • Persson K. Structure of the sortase AcSrtC-1 from Actinomyces oris. Acta Crystallogr D Biol Crystallogr 2011; 67(Pt 3): 212-217.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , Issue.PART 3 , pp. 212-217
    • Persson, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.