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| 001 | 166792 | ||
| 005 | 20250730152307.0 | ||
| 024 | 7 | _ | |a 10.1016/j.febslet.2013.07.038 |2 doi |
| 024 | 7 | _ | |a 1873-3468 |2 ISSN |
| 024 | 7 | _ | |a 0014-5793 |2 ISSN |
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| 037 | _ | _ | |a DESY-2014-01626 |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Eulenburg, Georg |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Structural and biochemical characterization of Rv2140c, a phosphatidylethanolamine-binding protein from Mycobacterium tuberculosis |
| 260 | _ | _ | |a Amsterdam [u.a.] |c 2013 |b Elsevier |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1529687264_1484 |2 PUB:(DE-HGF) |
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| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 500 | _ | _ | |a (c) Federation of European Biochemical Societies; Post referee fulltext in progress; Embargo 12 months from publication |
| 520 | _ | _ | |a 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. |
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| 700 | 1 | _ | |a Higman, Victoria A. |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Diehl, Anne |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Wilmanns, Matthias |0 P:(DE-H253)PIP1001283 |b 3 |
| 700 | 1 | _ | |a Holton, Simon J. |0 P:(DE-HGF)0 |b 4 |e Corresponding author |
| 773 | _ | _ | |a 10.1016/j.febslet.2013.07.038 |g Vol. 587, no. 18, p. 2936 - 2942 |0 PERI:(DE-600)1460391-3 |n 18 |p 2936 - 2942 |t FEBS letters |v 587 |y 2013 |x 0014-5793 |
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