1L6M

Neutrophil Gelatinase-associated Lipocalin is a Novel Bacteriostatic Agent that Interferes with Siderophore-mediated Iron Acquisition

Summary for 1L6M

• Entry DOI: 10.2210/pdb1l6m/pdb
• Related: 1dfv 1qqs
• Descriptor: Neutrophil gelatinase-associated lipocalin, FE (III) ION, SULFATE ION, ... (6 entities in total)
• Functional Keywords: lipocalin, siderophore, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P80188
• Total number of polymer chains: 3
• Total formula weight: 64051.61

Authors

Goetz, D.H.,Borregaard, N.,Bluhm, M.E.,Raymond, K.N.,Strong, R.K. (deposition date: 2002-03-11, release date: 2003-03-11, Last modification date: 2024-10-16)

Primary citation

Goetz, D.H.,Borregaard, N.,Bluhm, M.E.,Raymond, K.N.,Strong, R.K.
The Neutrophil Lipocalin NGAL is a Bacteriostatic Agent that Interferes with Siderophore-mediated Iron Acquisition
Mol.Cell, 10:1033-1043, 2002

PubMed Abstract: First identified as a neutrophil granule component, neutrophil gelatinase-associated lipocalin (NGAL; also called human neutrophil lipocalin, 24p3, uterocalin, or neu-related lipocalin) is a member of the lipocalin family of binding proteins. Putative NGAL ligands, including neutrophil chemotactic agents such as N-formylated tripeptides, have all been refuted by recent biochemical and structural results. NGAL has subsequently been implicated in diverse cellular processes, but without a characterized ligand, the molecular basis of these functions remained mysterious. Here we report that NGAL tightly binds bacterial catecholate-type ferric siderophores through a cyclically permuted, hybrid electrostatic/cation-pi interaction and is a potent bacteriostatic agent in iron-limiting conditions. We therefore propose that NGAL participates in the antibacterial iron depletion strategy of the innate immune system.

PubMed: 12453412
DOI: 10.1016/S1097-2765(02)00708-6

Experimental method

X-RAY DIFFRACTION (2.4 Å)