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. Author manuscript; available in PMC: 2016 Aug 31.
Published in final edited form as: Biochemistry. 2010 Mar 23;49(11):2368–2379. doi: 10.1021/bi901669q

Figure 3.

Figure 3

Gly88Ser and Gly88Thr PagP mutants reveal that polarity alone does not perturb acyl chain selection. (A) Far-UV CD identifies the β-barrel and exciton signatures characteristic of wild-type PagP. (B) Thermal melts at 218 nm reveal exciton loss preceding β-barrel unfolding. (C and D)Hydrocarbon ruler measurements reveal unitary acyl chain selectivity catalyzed by Gly88Ser and Gly88Thr PagP folded atpH8. Synthetic diacyl-PtdCho’s with saturated acyl chains varying in single increments from 10 to 17 carbon atoms were used as donors for the enzymatic acylation of Kdo2–lipid A. ND, not detected.