Structural and biochemical characterization of Rv2140c, a phosphatidylethanolamine‐binding protein from Mycobacterium tuberculosis. Issue 18 (29th July 2013)

• Record Type: Journal Article
• Authors: Eulenburg, Georg; Higman, Victoria A.; Diehl, Anne; Wilmanns, Matthias; Holton, Simon J.
• Is Part Of: FEBS letters. Volume 587:Issue 18(2013)
• Page Start: 2936
• Page End: 2942
• Publication Date: 2013-07-29
• Subjects: CR -- conserved region -- DHPE -- dihexanoyl phosphatidylethanolamine -- DHPG -- dihexanoyl phosphatidylglycerol -- DHPS -- dihexanoyl phosphatidylserine -- ITC -- isothermal titration calorimetry -- PE -- phosphatidylethanolamine -- PEBP -- phosphatidylethanolamine-binding protein -- PEBP -- Tuberculosis -- Structural biology; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.07.038
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : 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 . Abstract : Novel X‐ray structures of the Mtb Rv2140c protein in apo and sulfate‐bound forms. Rv2140c has strong structural homology to the phosphatidylethanolamine‐binding protein family. Rv2140c forms low‐millimolar interactions with soluble phosphatidylethanolamine analogs. The small molecule locostatin binds to the Rv2140c ligand‐binding site.