Acyl carrier proteins (ACPs) are small helical proteins found in all kingdoms of life, primarily involved in fatty acid and polyketide biosynthesis. In eukaryotes, ACPs are part of the fatty acid synthase (FAS) complex, where they act as flexible tethers for the growing lipid chain, enabling access to the distinct active sites in FAS. In the type II synthesis systems found in bacteria and plastids, these proteins exist as monomers and perform various processes, from being a donor for synthesis of various products such as endotoxins, to supplying acyl chains for lipid A and lipoic acid FAS (quorum sensing), but also as signaling molecules, in bioluminescence and activation of toxins. The essential and diverse nature of their functions makes ACP an attractive target for antimicrobial drug discovery. Here, we report the structure, dynamics and evolution of ACPs from three human pathogens: Borrelia burgdorferi, Brucella melitensis and Rickettsia prowazekii, which could facilitate the discovery of new inhibitors of ACP function in pathogenic bacteria.
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Cover Image
Prevotella intermedia PinO protein is homologous to Porphyromonas gingivalis HmuY hemophore-like protein, but binds haem with a different haem coordination mode and preferentially in reducing environment. Molecular dynamics stimulations of the haem iron coordination by the PinO suggest engagement of one methionine residue, with interchangeable participation of two additional methionine residues. For more information, see the article by Bielecki and colleagues on pp. 381–405. Image courtesy of Teresa Olczak.
Comparative structure, dynamics and evolution of acyl-carrier proteins from Borrelia burgdorferi, Brucella melitensis and Rickettsia prowazekii
Ravi P. Barnwal, Mandeep Kaur, Alec Heckert, Janeka Gartia, Gabriele Varani; Comparative structure, dynamics and evolution of acyl-carrier proteins from Borrelia burgdorferi, Brucella melitensis and Rickettsia prowazekii. Biochem J 31 January 2020; 477 (2): 491–508. doi: https://doi.org/10.1042/BCJ20190797
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