2LBV

Siderocalin Q83 reveals a dual ligand binding mode

Summary for 2LBV

• Entry DOI: 10.2210/pdb2lbv/pdb
• NMR Information: BMRB: 17577
• Descriptor: Extracellular fatty acid-binding protein, N,N',N''-[(3S,7S,11S)-2,6,10-trioxo-1,5,9-trioxacyclododecane-3,7,11-triyl]tris(2,3-dihydroxybenzamide), GALLIUM (III) ION, ... (4 entities in total)
• Functional Keywords: lipocalin, siderocalin, enterobactin, arachidonic acid, lipid transport
• Biological source: Coturnix japonica (Japanese quail)
• Cellular location: Secreted (By similarity): Q9I9P7
• Total number of polymer chains: 1
• Total formula weight: 19148.47

Authors

Coudevylle, N.,Hoetzinger, M.,Geist, L.,Kontaxis, G.,Bister, K.,Konrat, R. (deposition date: 2011-04-07, release date: 2012-02-22, Last modification date: 2024-11-20)

Primary citation

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, 50:9192-9199, 2011

PubMed Abstract: Siderocalins 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.

PubMed: 21951132
DOI: 10.1021/bi201115q

Experimental method

SOLUTION NMR