Open AccessNMR structure of an acyl‐carrier protein from Borrelia burgdorferi
Author(s) -
Barnwal Ravi P.,
Van Voorhis Wesley C.,
Varani G.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111004386
Subject(s) - aquifex aeolicus , structural genomics , borrelia burgdorferi , acyl carrier protein , nuclear magnetic resonance spectroscopy , protein structure , homology modeling , chemistry , crystallography , borrelia , stereochemistry , biochemistry , biology , biosynthesis , gene , genetics , enzyme , escherichia coli , antibody
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 .