4BEG

Structure of Rv2140c, a phosphatidyl-ethanolamine binding protein from Mycobacterium tuberculosis in complex with sulphate

Summary for 4BEG

• Entry DOI: 10.2210/pdb4beg/pdb
• Related: 4BEF
• Descriptor: PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: lipid-binding protein, pebp, rkip, lipid binding protein
• Biological source: MYCOBACTERIUM TUBERCULOSIS
• Total number of polymer chains: 2
• Total formula weight: 38300.69

Authors

Holton, S.J.,Williams, M. (deposition date: 2013-03-09, release date: 2013-08-14, Last modification date: 2023-12-20)

Primary citation

Eulenburg, G.,Higman, V.A.,Diehl, A.,Wilmanns, M.,Holton, S.J.
Structural and Biochemical Characterization of Rv2140C, a Phosphatidylethanolamine-Binding Protein from Mycobacterium Tuberculosis.
FEBS Lett., 587:2936-, 2013

PubMed 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.

PubMed: 23907008
DOI: 10.1016/J.FEBSLET.2013.07.038

Experimental method

X-RAY DIFFRACTION (1.42 Å)