TY  - JOUR
AU  - Eulenburg, Georg
AU  - Higman, Victoria A.
AU  - Diehl, Anne
AU  - Wilmanns, Matthias
AU  - Holton, Simon J.
TI  - Structural and biochemical characterization of Rv2140c, a phosphatidylethanolamine-binding protein from Mycobacterium tuberculosis
JO  - FEBS letters
VL  - 587
IS  - 18
SN  - 0014-5793
CY  - Amsterdam [u.a.]
PB  - Elsevier
M1  - DESY-2014-01626
SP  - 2936 - 2942
PY  - 2013
N1  - (c) Federation of European Biochemical Societies; Post referee fulltext in progress; Embargo 12 months from publication
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000324033700007
C6  - pmid:23907008
DO  - DOI:10.1016/j.febslet.2013.07.038
UR  - https://bib-pubdb1.desy.de/record/166792
ER  -