Advertisement

If you have an ACS member number, please enter it here so we can link this account to your membership. (optional)

ACS values your privacy. By submitting your information, you are gaining access to C&EN and subscribing to our weekly newsletter. We use the information you provide to make your reading experience better, and we will never sell your data to third party members.

ENJOY UNLIMITED ACCES TO C&EN

Biological Chemistry

Cell wall model proposed

March 13, 2006 | A version of this story appeared in Volume 84, Issue 11

The structure of the bacterial cell wall, which is a target for antibacterial drugs, has been difficult to clarify because of its complexity and the difficulty in obtaining individual components. The cell wall is formed from a peptidoglycan scaffold consisting of repeating disaccharide units of N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM), with a pentapeptide attached to each NAM. University of Notre Dame chemistry professor Shahriar Mobashery and coworkers have obtained a 3-D NMR structure of a 2-kilodalton synthetic fragment of this scaffold (Proc. Natl. Acad. Sci. USA, published online March 9, dx.doi.org/10.1073/pnas.0510182103). From this fragment, they predict that the longer native peptidoglycan strand is a right-handed helix with three repeats per turn and threefold symmetry along the helical axis; each strand can cross-link with up to three neighboring strands. They extrapolate to a model of the bacterial cell wall with a layered honeycomb pattern of varying pore sizes (top view shown), depending on the number of cross-links. Waldemar Vollmer of the University of Tübingen in Germany cautions that the model is "highly speculative" and "contradicts a number of experimental data."

Article:

This article has been sent to the following recipient:

0 /1 FREE ARTICLES LEFT THIS MONTH Remaining
Chemistry matters. Join us to get the news you need.