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@ARTICLE{Eulenburg:166792,
author = {Eulenburg, Georg and Higman, Victoria A. and Diehl, Anne
and Wilmanns, Matthias and Holton, Simon J.},
title = {{S}tructural and biochemical characterization of {R}v2140c,
a phosphatidylethanolamine-binding protein from
{M}ycobacterium tuberculosis},
journal = {FEBS letters},
volume = {587},
number = {18},
issn = {0014-5793},
address = {Amsterdam [u.a.]},
publisher = {Elsevier},
reportid = {DESY-2014-01626},
pages = {2936 - 2942},
year = {2013},
note = {(c) Federation of European Biochemical Societies; Post
referee fulltext in progress; Embargo 12 months from
publication},
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.},
cin = {EMBL},
ddc = {570},
cid = {I:(DE-H253)EMBL-20120731},
pnm = {DORIS Beamline BW7 (POF2-54G13)},
pid = {G:(DE-H253)POF2-BW7-20130405},
experiment = {EXP:(DE-H253)D-BW7-20150101},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000324033700007},
pubmed = {pmid:23907008},
doi = {10.1016/j.febslet.2013.07.038},
url = {https://bib-pubdb1.desy.de/record/166792},
}