Structural highlights
Function
EXFAB_COTJA Siderocalin-like lipocalin tightly binding a variety of bacterial ferric siderophores, also binds long-chain unsaturated fatty acids such as linoleic acid, oleic acid, arachidonic acid and, with a lower affinity, long chain saturated fatty acids such as steraic acid. May act as an antibacterial factor, through dual ligand specificity, both as a siderophore-sequestrating molecule and a lysophosphatidic acid (LPA) sensor.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Coudevylle N, Geist L, Hotzinger M, Hartl M, Kontaxis G, Bister K, Konrat R. The v-myc-induced Q83 lipocalin is a siderocalin. J Biol Chem. 2010 Dec 31;285(53):41646-52. Epub 2010 Sep 8. PMID:20826777 doi:10.1074/jbc.M110.123331
- ↑ Coudevylle N, Hoetzinger M, Geist L, Kontaxis G, Hartl M, Bister K, Konrat R. Lipocalin Q83 reveals a dual ligand binding mode with potential implications for the functions of siderocalins. Biochemistry. 2011 Nov 1;50(43):9192-9. Epub 2011 Oct 7. PMID:21951132 doi:http://dx.doi.org/10.1021/bi201115q
