6O5D

PYOCHELIN

「3U03」から置き換えられました

6O5D の概要

• エントリーDOI: 10.2210/pdb6o5d/pdb
• 分子名称: Neutrophil gelatinase-associated lipocalin, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: beta-barrel, siderocalin, antimicrobial protein, structural genomics, seattle structural genomics center for infectious disease, ssgcid, transport protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 61039.61

構造登録者

Rupert, P.B.,Strong, R.K.,Clifton, M.C.,Edwards, T.E.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2019-03-01, 公開日: 2019-09-11, 最終更新日: 2024-11-20)

主引用文献

Clifton, M.C.,Rupert, P.B.,Hoette, T.M.,Raymond, K.N.,Abergel, R.J.,Strong, R.K.
Parsing the functional specificity of Siderocalin/Lipocalin 2/NGAL for siderophores and related small-molecule ligands.
J Struct Biol X, 2:100008-100008, 2019

PubMed Abstract: Siderocalin/Lipocalin 2/Neutrophil Gelatinase Associated Lipocalin/24p3 is an innate immune system protein with bacteriostatic activity, acting by tightly binding and sequestering diverse catecholate and mixed-type ferric siderophores from enteric bacteria and mycobacteria. Bacterial virulence achieved through siderophore modifications, or utilization of alternate siderophores, can be explained by evasion of Siderocalin binding. Siderocalin has also been implicated in a wide variety of disease processes, though often in seemingly contradictory ways, and has been proposed to bind to a broader array of ligands beyond siderophores. Using structural, directed mutational, and binding studies, we have sought to rigorously test, and fully elucidate, the Siderocalin recognition mechanism. Several proposed ligands fail to meet rigorous binding criteria, including the bacterial siderophore pyochelin, the iron-chelating catecholamine hormone norepinephrine, and the bacterial second messenger cyclic diguanylate monophosphate. While possessing a remarkably rigid structure, in principle simplifying analyses of ligand recognition, understanding Scn recognition is complicated by the observed conformational and stoichiometric plasticity, and instability, of its siderophore ligands. Since the role of Siderocalin at the early host/pathogen interface is to compete for bacterial ferric siderophores, we also analyzed how bacterial siderophore binding proteins and enzymes alternately recognize siderophores that efficiently bind to, or evade, Siderocalin sequestration - including determining the crystal structure of YfiY bound to schizokinen. These studies combine to refine the potential physiological functions of Siderocalin by defining its multiplexed recognition mechanism.

PubMed: 32647813
DOI: 10.1016/j.yjsbx.2019.100008

実験手法

X-RAY DIFFRACTION (2.4 Å)