Characterization of the structure and catalytic activity of Legionella pneumophila VipF.

Autor: Young BH; Department of Chemistry and Biochemistry, James Madison University, Harrisonburg, Virginia, 22807., Caldwell TA; Department of Chemistry and Biochemistry, James Madison University, Harrisonburg, Virginia, 22807., McKenzie AM; Department of Chemistry and Biochemistry, James Madison University, Harrisonburg, Virginia, 22807., Kokhan O; Department of Chemistry and Biochemistry, James Madison University, Harrisonburg, Virginia, 22807., Berndsen CE; Department of Chemistry and Biochemistry, James Madison University, Harrisonburg, Virginia, 22807. berndsce@jmu.edu.
Jazyk: angličtina
Zdroj: Proteins [Proteins] 2016 Oct; Vol. 84 (10), pp. 1422-30. Date of Electronic Publication: 2016 Jul 05.
DOI: 10.1002/prot.25087
Abstrakt: The pathogenic bacteria Legionella pneumophila is known to cause Legionnaires' Disease, a severe pneumonia that can be fatal to immunocompromised individuals and the elderly. Shohdy et al. identified the L. pneumophila vacuole sorting inhibitory protein VipF as a putative N-acetyltransferase based on sequence homology. We have characterized the basic structural and functional properties of VipF to confirm this original functional assignment. Sequence conservation analysis indicates two putative CoA-binding regions within VipF. Homology modeling and small angle X-ray scattering suggest a monomeric, dual-domain structure joined by a flexible linker. Each domain contains the characteristic beta-splay motif found in many acetyltransferases, suggesting that VipF may contain two active sites. Docking experiments suggest reasonable acetyl-CoA binding locations within each beta-splay motif. Broad substrate screening indicated that VipF is capable of acetylating chloramphenicol and both domains are catalytically active. Given that chloramphenicol is not known to be N-acetylated, this is a surprising finding suggesting that VipF is capable of O-acetyltransferase activity. Proteins 2016; 84:1422-1430. © 2016 Wiley Periodicals, Inc.
(© 2016 Wiley Periodicals, Inc.)
Databáze: MEDLINE
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