NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
 

NMR structure of an acyl-carrier protein from Borrelia burgdorferi.

NMR structure of an acyl-carrier protein from Borrelia burgdorferi.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt 9):1137-40

Authors: Barnwal RP, Van Voorhis WC, Varani G

Abstract
Nearly complete resonance assignment and the high-resolution NMR structure of the acyl-carrier protein from Borrelia burgdorferi, a target of the Seattle Structural Genomics Center for Infectious Disease (SSGCID) structure-determination pipeline, are reported. This protein was chosen as a potential target for drug-discovery efforts because of its involvement in fatty-acid biosynthesis, an essential metabolic pathway, in bacteria. It was possible to assign >98% of backbone resonances and >92% of side-chain resonances using multidimensional NMR spectroscopy. The NMR structure was determined to a backbone r.m.s.d. of 0.4 Å and contained four ?-helices and two 3(10)-helices. A structure-homology search revealed that this protein is highly similar to the acyl-carrier protein from Aquifex aeolicus.


PMID: 21904063 [PubMed - in process]



Source: PubMed