Structural highlights
Publication Abstract from PubMed
CapE is an essential enzyme for the synthesis of capsular polysaccharide (CP) of pathogenic strains of Staphylococcus aureus. Herein we demonstrate that CapE is a 5-inverting 4,6-dehydratase enzyme. However, in the absence of downstream enzymes, CapE catalyzes an additional reaction (5-back-epimerization) affording a by-product under thermodynamic control. Single-crystal X-ray crystallography was employed to identify the structure of the by-product. The structural analysis reveals a network of coordinated motions away from the active site governing the enzymatic activity of CapE. A second dynamic element (the latch) regulates the enzymatic chemoselectivity. The validity of these mechanisms was evaluated by site-directed mutagenesis.
Dynamic elements govern the catalytic activity of CapE, a capsular polysaccharide-synthesizing enzyme from Staphylococcus aureus.,Miyafusa T, Caaveiro JM, Tanaka Y, Tsumoto K FEBS Lett. 2013 Oct 21. pii: S0014-5793(13)00766-7. doi:, 10.1016/j.febslet.2013.10.009. PMID:24157361[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Miyafusa T, Caaveiro JM, Tanaka Y, Tsumoto K. Dynamic elements govern the catalytic activity of CapE, a capsular polysaccharide-synthesizing enzyme from Staphylococcus aureus. FEBS Lett. 2013 Oct 21. pii: S0014-5793(13)00766-7. doi:, 10.1016/j.febslet.2013.10.009. PMID:24157361 doi:http://dx.doi.org/10.1016/j.febslet.2013.10.009
