2lbv
From Proteopedia
Siderocalin Q83 reveals a dual ligand binding mode
Structural highlights
FunctionEXFAB_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] Publication Abstract from PubMedSiderocalins are particular lipocalins that participate in the innate immune response by interfering with bacterial siderophore-mediated iron uptake. Additionally, siderocalins are involved in several physiological and pathological processes such as inflammation, iron delivery, tissue differentiation, and cancer progression. Here we show that siderocalin Q83 displays an unexpected dual ligand binding mode as it can bind enterobactin and unsaturated fatty acids simultaneously. The solution structure of the siderocalin Q83 in complex with arachidonic acid and enterobactin reveals molecular details of this novel dual binding mode and the determinants of fatty acid binding specificity. Our results suggest that Q83 is a metabolic hub linking iron and fatty acid pathways. This unexpected coupling might contribute to the pleiotropic functions of siderocalins. Lipocalin Q83 reveals a dual ligand binding mode with potential implications for the functions of siderocalins.,Coudevylle N, Hoetzinger M, Geist L, Kontaxis G, Hartl M, Bister K, Konrat R Biochemistry. 2011 Nov 1;50(43):9192-9. Epub 2011 Oct 7. PMID:21951132[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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