Labischinski H, Barnickel G, Naumann D, Keller P
Ann Inst Pasteur Microbiol (1985). 1985 Jan-Feb;136A(1):45-50. doi: 10.1016/s0769-2609(85)80020-x.
An atomic model of the conformation of peptidoglycan was taken as the basis for an analysis of packing patterns of the peptidoglycan strands in two- and three-dimensional arrangements. For the sake of clarity, glycan strands were approximated by cylindrical rods around which a continuous helix of possible peptide cross-linkage sites was arranged. Using the packing patterns obtained, several important properties of the murein network could be explained. These include variations in the degree of cross-linking in Gram-negative and Gram-positive bacteria and an estimation of the number of peptide monomers, di/trimers and oligomers present. Furthermore, our model is compatible with the well known flexibility of the murein fabric and the distinct elastic properties of the cell wall in gram-positive cocci and rod-shaped bacteria.
肽聚糖构象的原子模型被用作分析二维和三维排列中肽聚糖链堆积模式的基础。为了清晰起见，聚糖链由圆柱形杆近似表示，围绕这些杆排列着可能的肽交联位点的连续螺旋。利用获得的堆积模式，可以解释胞壁质网络的几个重要特性。这些特性包括革兰氏阴性菌和革兰氏阳性菌交联程度的变化，以及对存在的肽单体、二聚体/三聚体和寡聚体数量的估计。此外，我们的模型与众所周知的胞壁质结构的柔韧性以及革兰氏阳性球菌和杆状细菌细胞壁独特的弹性特性相兼容。
