2KWL

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

(2011) Acta Crystallogr Sect F Struct Biol Cryst Commun 67: 1137-1140

• PubMed: 21904063 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1107/S1744309111004386
• Primary Citation of Related Structures:  
  2KWL


• PubMed 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 α-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.

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Organizational Affiliation: 

Department of Chemistry, University of Washington, Seattle, WA 98195, USA.