Structural highlights
Publication Abstract from PubMed
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.
Structural and biochemical characterization of Rv2140c, a phosphatidylethanolamine-binding protein from Mycobacterium tuberculosis.,Eulenburg G, Higman VA, Diehl A, Wilmanns M, Holton SJ FEBS Lett. 2013 Jul 29. pii: S0014-5793(13)00567-X. doi:, 10.1016/j.febslet.2013.07.038. PMID:23907008[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Eulenburg G, Higman VA, Diehl A, Wilmanns M, Holton SJ. Structural and biochemical characterization of Rv2140c, a phosphatidylethanolamine-binding protein from Mycobacterium tuberculosis. FEBS Lett. 2013 Jul 29. pii: S0014-5793(13)00567-X. doi:, 10.1016/j.febslet.2013.07.038. PMID:23907008 doi:10.1016/j.febslet.2013.07.038
