메뉴 건너뛰기




Volumn 383, Issue 1, 2008, Pages 167-177

Identification of Dynamic Structural Motifs Involved in Peptidoglycan Glycosyltransfer

Author keywords

crystal structure; glycosyltransferase; penicillin; peptidoglycan; bulge

Indexed keywords

EXOMURAMIDASE; LYSOZYME; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 52049104949     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.08.020     Document Type: Article
Times cited : (44)

References (32)
  • 1
    • 0142126675 scopus 로고    scopus 로고
    • Bacterial wall as target for attack: past, present, and future research
    • Koch A.L. Bacterial wall as target for attack: past, present, and future research. Clin. Microbiol. Rev. 16 (2003) 673-687
    • (2003) Clin. Microbiol. Rev. , vol.16 , pp. 673-687
    • Koch, A.L.1
  • 2
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Holtje J.V. Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol. Mol. Biol. Rev. 62 (1998) 181-203
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 181-203
    • Holtje, J.V.1
  • 3
    • 33645084237 scopus 로고    scopus 로고
    • Future chemotherapy, with emphasis on bacterial murein
    • Koch A.L. Future chemotherapy, with emphasis on bacterial murein. FEMS Immunol. Med. Microbiol. 46 (2006) 158-165
    • (2006) FEMS Immunol. Med. Microbiol. , vol.46 , pp. 158-165
    • Koch, A.L.1
  • 4
    • 0031736387 scopus 로고    scopus 로고
    • Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs
    • Goffin C., and Ghuysen J.M. Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. 62 (1998) 1079-1093
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1079-1093
    • Goffin, C.1    Ghuysen, J.M.2
  • 5
    • 33947132188 scopus 로고    scopus 로고
    • Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis
    • Lovering A.L., de Castro L.H., Lim D., and Strynadka N.C. Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis. Science 315 (2007) 1402-1405
    • (2007) Science , vol.315 , pp. 1402-1405
    • Lovering, A.L.1    de Castro, L.H.2    Lim, D.3    Strynadka, N.C.4
  • 6
    • 34248400401 scopus 로고    scopus 로고
    • Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis
    • Yuan Y., Barrett D., Zhang Y., Kahne D., Sliz P., and Walker S. Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis. Proc. Natl Acad. Sci. USA 104 (2007) 5348-5353
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 5348-5353
    • Yuan, Y.1    Barrett, D.2    Zhang, Y.3    Kahne, D.4    Sliz, P.5    Walker, S.6
  • 7
    • 35548940362 scopus 로고    scopus 로고
    • The direction of glycan chain elongation by peptidoglycan glycosyltransferases
    • Perlstein D.L., Zhang Y., Wang T.S., Kahne D.E., and Walker S. The direction of glycan chain elongation by peptidoglycan glycosyltransferases. J. Am. Chem. Soc. 129 (2007) 12674-12675
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 12674-12675
    • Perlstein, D.L.1    Zhang, Y.2    Wang, T.S.3    Kahne, D.E.4    Walker, S.5
  • 8
    • 0027467033 scopus 로고
    • The alpha aneurism: a structural motif revealed in an insertion mutant of staphylococcal nuclease
    • Keefe L.J., Sondek J., Shortle D., and Lattman E.E. The alpha aneurism: a structural motif revealed in an insertion mutant of staphylococcal nuclease. Proc. Natl Acad. Sci. USA 90 (1993) 3275-3279
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 3275-3279
    • Keefe, L.J.1    Sondek, J.2    Shortle, D.3    Lattman, E.E.4
  • 10
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme
    • Hayward S., and Berendsen H.J. Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme. Proteins 30 (1998) 144-154
    • (1998) Proteins , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.2
  • 11
    • 0028874610 scopus 로고
    • Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A. Implications for the enzymatic mechanism
    • Thunnissen A.M., Rozeboom H.J., Kalk K.H., and Dijkstra B.W. Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A. Implications for the enzymatic mechanism. Biochemistry 34 (1995) 12729-12737
    • (1995) Biochemistry , vol.34 , pp. 12729-12737
    • Thunnissen, A.M.1    Rozeboom, H.J.2    Kalk, K.H.3    Dijkstra, B.W.4
  • 13
    • 0016726181 scopus 로고
    • Novel type of murein transglycosylase in Escherichia coli
    • Holtje J.V., Mirelman D., Sharon N., and Schwarz U. Novel type of murein transglycosylase in Escherichia coli. J. Bacteriol. 124 (1975) 1067-1076
    • (1975) J. Bacteriol. , vol.124 , pp. 1067-1076
    • Holtje, J.V.1    Mirelman, D.2    Sharon, N.3    Schwarz, U.4
  • 14
    • 0033609769 scopus 로고    scopus 로고
    • High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment
    • van Asselt E.J., Thunnissen A.M., and Dijkstra B.W. High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment. J. Mol. Biol. 291 (1999) 877-898
    • (1999) J. Mol. Biol. , vol.291 , pp. 877-898
    • van Asselt, E.J.1    Thunnissen, A.M.2    Dijkstra, B.W.3
  • 15
    • 0025012287 scopus 로고
    • Isolation and separation of the glycan strands from murein of Escherichia coli by reversed-phase high-performance liquid chromatography
    • Harz H., Burgdorf K., and Holtje J.V. Isolation and separation of the glycan strands from murein of Escherichia coli by reversed-phase high-performance liquid chromatography. Anal. Biochem. 190 (1990) 120-128
    • (1990) Anal. Biochem. , vol.190 , pp. 120-128
    • Harz, H.1    Burgdorf, K.2    Holtje, J.V.3
  • 16
    • 31344459535 scopus 로고    scopus 로고
    • Native cell wall organization shown by cryo-electron microscopy confirms the existence of a periplasmic space in Staphylococcus aureus
    • Matias V.R., and Beveridge T.J. Native cell wall organization shown by cryo-electron microscopy confirms the existence of a periplasmic space in Staphylococcus aureus. J. Bacteriol. 188 (2006) 1011-1021
    • (2006) J. Bacteriol. , vol.188 , pp. 1011-1021
    • Matias, V.R.1    Beveridge, T.J.2
  • 17
    • 39749105962 scopus 로고    scopus 로고
    • The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with the penicillin-binding protein 3 (PBP3), FtsW and FtsN
    • Derouaux A., Wolf B., Fraipont C., Breukink E., Nguyen-Disteche M., and Terrak M. The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with the penicillin-binding protein 3 (PBP3), FtsW and FtsN. J. Bacteriol. 190 (2007) 1831-1834
    • (2007) J. Bacteriol. , vol.190 , pp. 1831-1834
    • Derouaux, A.1    Wolf, B.2    Fraipont, C.3    Breukink, E.4    Nguyen-Disteche, M.5    Terrak, M.6
  • 18
    • 27844575191 scopus 로고    scopus 로고
    • In vitro murein peptidoglycan synthesis by dimers of the bifunctional transglycosylase-transpeptidase PBP1B from Escherichia coli
    • Bertsche U., Breukink E., Kast T., and Vollmer W. In vitro murein peptidoglycan synthesis by dimers of the bifunctional transglycosylase-transpeptidase PBP1B from Escherichia coli. J. Biol. Chem. 280 (2005) 38096-38101
    • (2005) J. Biol. Chem. , vol.280 , pp. 38096-38101
    • Bertsche, U.1    Breukink, E.2    Kast, T.3    Vollmer, W.4
  • 19
    • 0028904640 scopus 로고
    • Differences between inner membrane and peptidoglycan-associated PBP1B dimers of Escherichia coli
    • Zijderveld C.A., Aarsman M.E., and Nanninga N. Differences between inner membrane and peptidoglycan-associated PBP1B dimers of Escherichia coli. J. Bacteriol. 177 (1995) 1860-1863
    • (1995) J. Bacteriol. , vol.177 , pp. 1860-1863
    • Zijderveld, C.A.1    Aarsman, M.E.2    Nanninga, N.3
  • 21
    • 34548438988 scopus 로고    scopus 로고
    • High-resolution structure of the major periplasmic domain from the cell shape-determining filament MreC
    • Lovering A.L., and Strynadka N.C. High-resolution structure of the major periplasmic domain from the cell shape-determining filament MreC. J. Mol. Biol. 372 (2007) 1034-1044
    • (2007) J. Mol. Biol. , vol.372 , pp. 1034-1044
    • Lovering, A.L.1    Strynadka, N.C.2
  • 22
    • 50049104157 scopus 로고    scopus 로고
    • Vollmer, W. & Bertsche, U. (2007). Murein (peptido-glycan) structure, architecture and biosynthesis in Escherichia coli. Biochim. Biophys. Acta. In press. doi:10.1016/j.bbamem.2007.06.007.
    • Vollmer, W. & Bertsche, U. (2007). Murein (peptido-glycan) structure, architecture and biosynthesis in Escherichia coli. Biochim. Biophys. Acta. In press. doi:10.1016/j.bbamem.2007.06.007.
  • 23
    • 0034602394 scopus 로고    scopus 로고
    • Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I
    • Pedersen L.C., Tsuchida K., Kitagawa H., Sugahara K., Darden T.A., and Negishi M. Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I. J. Biol. Chem. 275 (2000) 34580-34585
    • (2000) J. Biol. Chem. , vol.275 , pp. 34580-34585
    • Pedersen, L.C.1    Tsuchida, K.2    Kitagawa, H.3    Sugahara, K.4    Darden, T.A.5    Negishi, M.6
  • 24
    • 0033556340 scopus 로고    scopus 로고
    • Moenomycin A: the role of the methyl group in the moenuronamide unit and a general discussion of structure-activity relationships
    • Ei-Abadla N., Lampilas M., Hennig L., Findeisen M., Welzel P., Muller D., et al. Moenomycin A: the role of the methyl group in the moenuronamide unit and a general discussion of structure-activity relationships. Tetrahedron 55 (1999) 699-722
    • (1999) Tetrahedron , vol.55 , pp. 699-722
    • Ei-Abadla, N.1    Lampilas, M.2    Hennig, L.3    Findeisen, M.4    Welzel, P.5    Muller, D.6
  • 25
    • 0037417869 scopus 로고    scopus 로고
    • Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases
    • Hu Y., Chen L., Ha S., Gross B., Falcone B., Walker D., et al. Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases. Proc. Natl Acad. Sci. USA 100 (2003) 845-849
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 845-849
    • Hu, Y.1    Chen, L.2    Ha, S.3    Gross, B.4    Falcone, B.5    Walker, D.6
  • 27
    • 0032512617 scopus 로고    scopus 로고
    • Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes
    • Evrard C., Fastrez J., and Declercq J.P. Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes. J. Mol. Biol. 276 (1998) 151-164
    • (1998) J. Mol. Biol. , vol.276 , pp. 151-164
    • Evrard, C.1    Fastrez, J.2    Declercq, J.P.3
  • 28
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 29
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy A.J. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr., Sect. D: Biol. Crystallogr. 63 (2007) 32-41
    • (2007) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 32
    • 0003845223 scopus 로고    scopus 로고
    • DeLano Scientific, Palo Alto, CA http://www.pymol.org
    • DeLano W.L. The PyMOL Molecular Graphics System (2002), DeLano Scientific, Palo Alto, CA. http://www.pymol.org http://www.pymol.org
    • (2002) The PyMOL Molecular Graphics System
    • DeLano, W.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.