The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase.

ABSTRACT: Lipoic acid is essential for the activation of a number of protein complexes involved in key metabolic processes. Growth of Mycobacterium tuberculosis relies on a pathway in which the lipoate attachment group is synthesized from an endogenously produced octanoic acid moiety. In patients with multiple-drug-resistant M. tuberculosis, expression of one gene from this pathway, lipB, encoding for octanoyl-[acyl carrier protein]-protein acyltransferase is considerably up-regulated, thus making it a potential target in the search for novel antiinfectives against tuberculosis. Here we present the crystal structure of the M. tuberculosis LipB protein at atomic resolution, showing an unexpected thioether-linked active-site complex with decanoic acid. We provide evidence that the transferase function

SUBMITTER: Ma Q 

PROVIDER: S-EPMC1472244 | biostudies-literature | 2006 Jun

REPOSITORIES: biostudies-literature