Journal Article

DESY-2014-01626

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structural and biochemical characterization of Rv2140c, a phosphatidylethanolamine-binding protein from Mycobacterium tuberculosis

Eulenburg, G.>EMBL* ; Higman, V. A. ; Diehl, A. ; Wilmanns, M.Extern*>EMBL* ; Holton, S. J. (Corresponding author)

2013
Elsevier Amsterdam [u.a.]

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Please use a persistent id in citations: doi:10.1016/j.febslet.2013.07.038

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.

Note: (c) Federation of European Biochemical Societies; Post referee fulltext in progress; Embargo 12 months from publication

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Contributing Institute(s):

1. EMBL (EMBL)

Research Program(s):

1. DORIS Beamline BW7 (POF2-54G13) (POF2-54G13)

Experiment(s):

1. DORIS Beamline BW7 (DORIS III)

Appears in the scientific report 2013

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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