3U0D

The structure of human Siderocalin bound to the bacterial siderophore 2,3-DHBA

Summary for 3U0D

• Entry DOI: 10.2210/pdb3u0d/pdb
• Descriptor: Neutrophil gelatinase-associated lipocalin, FE (III) ION, 2,3-DIHYDROXY-BENZOIC ACID, ... (5 entities in total)
• Functional Keywords: siderophore, beta-barrel, structural genomics, seattle structural genomics center for infectious disease, ssgcid, transport protein, antimicrobial protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted : P80188
• Total number of polymer chains: 4
• Total formula weight: 92571.03

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2011-09-28, release date: 2011-10-12, Last modification date: 2024-11-06)

Primary citation

Correnti, C.,Richardson, V.,Sia, A.K.,Bandaranayake, A.D.,Ruiz, M.,Suryo Rahmanto, Y.,Kovacevic, Z.,Clifton, M.C.,Holmes, M.A.,Kaiser, B.K.,Barasch, J.,Raymond, K.N.,Richardson, D.R.,Strong, R.K.
Siderocalin/Lcn2/NGAL/24p3 does not drive apoptosis through gentisic acid mediated iron withdrawal in hematopoietic cell lines.
Plos One, 7:e43696-e43696, 2012

PubMed Abstract: Siderocalin (also lipocalin 2, NGAL or 24p3) binds iron as complexes with specific siderophores, which are low molecular weight, ferric ion-specific chelators. In innate immunity, siderocalin slows the growth of infecting bacteria by sequestering bacterial ferric siderophores. Siderocalin also binds simple catechols, which can serve as siderophores in the damaged urinary tract. Siderocalin has also been proposed to alter cellular iron trafficking, for instance, driving apoptosis through iron efflux via BOCT. An endogenous siderophore composed of gentisic acid (2,5-dihydroxybenzoic acid) substituents was proposed to mediate cellular efflux. However, binding studies reported herein contradict the proposal that gentisic acid forms high-affinity ternary complexes with siderocalin and iron, or that gentisic acid can serve as an endogenous siderophore at neutral pH. We also demonstrate that siderocalin does not induce cellular iron efflux or stimulate apoptosis, questioning the role siderocalin plays in modulating iron metabolism.

PubMed: 22928018
DOI: 10.1371/journal.pone.0043696

Experimental method

X-RAY DIFFRACTION (2.51 Å)