by Hans H. Martin
Isolated peptidoglycan sacculi from Aqua-
spirillum serpens.
In my retirement, one topic that continues to interest me is the 3D-structure of murein (i.e., peptidogylcan, as is now generally preferred in the literature). I participated in the isolation and description of the "murein sacculus," the "little sac" of E. coli B, under the directorship of Wolfhard Weidel in Tübingen, Germany, in the late 1950's and early 60's. An old review (Bag-shaped Macromolecules: A New Outlook on Bacterial Cell Walls) presented the concept that the bacterial exoskeleton is "a rigid bag of the shape and volume of the cell" in the form of "one enormous macromolecule kept together by covalent bonds throughout." The authors included a simple hypothetical model for the structure of the sacculus.
During the past 40 years, a considerable number of increasingly sophisticated and ingenious studies of 3D-peptidoglycan structure have been presented and different models have been proposed. Regular or irregular, parallel or perpendicular orientation of peptidoglycan strands to the cell surface were considered. (For three more recent papers, click here, here, and here.) But invariably, the authors have accepted that this is "one of the most important, yet still unsolved, structural problems in biochemistry." They concluded that "there is a shortage of methods by which to determine precisely, by direct structural analysis, the tertiary structure of peptidoglycan." However, very recently Grant Jensen and co-workers at Caltech reported an important advance in visualizing structural details in peptidoglycan from Gram-negative bacteria.