Three-dimensional structure of the bacterial cell wall peptidoglycan

被引:307
作者
Meroueh, SO
Bencze, KZ
Hesek, D
Lee, M
Fisher, JF
Stemmler, TL
Mobashery, S [1 ]
机构
[1] Univ Notre Dame, Dept Chem & Biochem, Notre Dame, IN 46556 USA
[2] Wayne State Univ, Sch Med, Dept Biochem, Detroit, MI 48201 USA
关键词
murein sacculus; bacterial envelope;
D O I
10.1073/pnas.0510182103
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The 3D structure of the bacterial peptidoglycan, the major constituent of the cell wall, is one of the most important, yet still unsolved, structural problems in biochemistry. The peptidoglycan comprises alternating N-acetylglucosamine (NAG) and N-acetylmuramic disaccharide (NAM) saccharides, the latter of which has a peptide stem. Adjacent peptide stems are cross-linked by the transpeptidase enzymes of cell wall biosynthesis to provide the cell wall polymer with the structural integrity required by the bacterium. The cell wall and its biosynthetic enzymes are targets of antibiotics. The 3D structure of the cell wall has been elusive because of its complexity and the lack of pure samples. Herein we report the 3D solution structure as determined by NMR of the 2-kDa NAG-NAM(pentapeptide)-NAG-NAM(pentapeptide) synthetic fragment of the cell wall. The glycan backbone of this peptidoglycan forms a right-handed helix with a periodicity of three for the NAG-NAM repeat (per turn of the helix). The first two amino acids of the pentapeptide adopt a limited number of conformations. Based on this structure a model for the bacterial cell wall is proposed.
引用
收藏
页码:4404 / 4409
页数:6
相关论文
共 49 条
[1]   NMR and modeling studies of protein-carbohydrate interactions:: Synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides [J].
Aboitiz, N ;
Vila-Perelló, M ;
Groves, P ;
Asensio, JL ;
Andreu, D ;
Cañada, FJ ;
Jiménez-Barbero, J .
CHEMBIOCHEM, 2004, 5 (09) :1245-1255
[2]   Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa -: Dual modes of membrane anchoring and occluded cavity end [J].
Akama, H ;
Kanemaki, M ;
Yoshimura, M ;
Tsukihara, T ;
Kashiwagi, T ;
Yoneyama, H ;
Narita, S ;
Nakagawa, A ;
Nakae, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (51) :52816-52819
[3]   New insight into cellulose structure by atomic force microscopy shows the Iα crystal phase at near-atomic resolution [J].
Baker, AA ;
Helbert, W ;
Sugiyama, J ;
Miles, MJ .
BIOPHYSICAL JOURNAL, 2000, 79 (02) :1139-1145
[4]   THE PROGRAM XEASY FOR COMPUTER-SUPPORTED NMR SPECTRAL-ANALYSIS OF BIOLOGICAL MACROMOLECULES [J].
BARTELS, C ;
XIA, TH ;
BILLETER, M ;
GUNTERT, P ;
WUTHRICH, K .
JOURNAL OF BIOMOLECULAR NMR, 1995, 6 (01) :1-10
[5]   Generalized born models of macromolecular solvation effects [J].
Bashford, D ;
Case, DA .
ANNUAL REVIEW OF PHYSICAL CHEMISTRY, 2000, 51 :129-152
[6]   Structures of gram-negative cell walls and their derived membrane vesicles [J].
Beveridge, TJ .
JOURNAL OF BACTERIOLOGY, 1999, 181 (16) :4725-4733
[7]   STRUCTURE OF PEPTIDOGLYCAN OF BACTERIAL-CELL WALLS .1. [J].
BURGE, RE ;
FOWLER, AG ;
REAVELEY, DA .
JOURNAL OF MOLECULAR BIOLOGY, 1977, 117 (04) :927-953
[8]   Bacterial cell shape [J].
Cabeen, MT ;
Jacobs-Wagner, C .
NATURE REVIEWS MICROBIOLOGY, 2005, 3 (08) :601-610
[9]  
Case D.A., 2002, AMBER 7
[10]  
CAVANAGH J, 1995, PROTEIN NMR SPECTROS