%0 Journal Article
%A Eulenburg, Georg
%A Higman, Victoria A.
%A Diehl, Anne
%A Wilmanns, Matthias
%A Holton, Simon J.
%T Structural and biochemical characterization of Rv2140c, a phosphatidylethanolamine-binding protein from Mycobacterium tuberculosis
%J FEBS letters
%V 587
%N 18
%@ 0014-5793
%C Amsterdam [u.a.]
%I Elsevier
%M DESY-2014-01626
%P 2936 - 2942
%D 2013
%Z (c) Federation of European Biochemical Societies; Post referee fulltext in progress; Embargo 12 months from publication
%X Rv2140c is one of many conserved Mycobacterium tuberculosis proteins for which no molecular function has been identified. We have determined a high-resolution crystal structure of the Rv2140c gene product, which reveals a dimeric complex that shares strong structural homology with the phosphatidylethanolamine-binding family of proteins. Rv2140c forms low-millimolar interactions with a selection of soluble phosphatidylethanolamine analogs, indicating that it has a role in lipid metabolism. Furthermore, the small molecule locostatin binds to the Rv2140c ligand-binding site and also inhibits the growth of the model organism Mycobacterium smegmatis.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000324033700007
%$ pmid:23907008
%R 10.1016/j.febslet.2013.07.038
%U https://bib-pubdb1.desy.de/record/166792