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000166792 1001_ $$0P:(DE-HGF)0$$aEulenburg, Georg$$b0
000166792 245__ $$aStructural and biochemical characterization of Rv2140c, a phosphatidylethanolamine-binding protein from Mycobacterium tuberculosis
000166792 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2013
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000166792 520__ $$aRv2140c 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.
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000166792 7001_ $$0P:(DE-HGF)0$$aHigman, Victoria A.$$b1
000166792 7001_ $$0P:(DE-HGF)0$$aDiehl, Anne$$b2
000166792 7001_ $$0P:(DE-H253)PIP1001283$$aWilmanns, Matthias$$b3
000166792 7001_ $$0P:(DE-HGF)0$$aHolton, Simon J.$$b4$$eCorresponding author
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