3UAQ

Crystal Structure of the N-lobe Domain of Lactoferrin Binding Protein B (LbpB) of Moraxella bovis

3UAQ の概要

• エントリーDOI: 10.2210/pdb3uaq/pdb
• 分子名称: LbpB B-lobe (1 entity in total)
• 機能のキーワード: beta barrel, lipoprotein, protein binding
• 由来する生物種: Moraxella bovis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74994.30

構造登録者

Arutyunova, E.,Brooks, C.L.,Beddeck, A.,Mak, M.W.,Schryvers, A.B.,Lemieux, M.J. (登録日: 2011-10-21, 公開日: 2012-03-28, 最終更新日: 2023-09-13)

主引用文献

Arutyunova, E.,Brooks, C.L.,Beddek, A.,Mak, M.W.,Schryvers, A.B.,Lemieux, M.J.
Crystal structure of the N-lobe of lactoferrin binding protein B from Moraxella bovis(1).
Biochem.Cell Biol., 90:351-361, 2012

PubMed Abstract: Lactoferrin (Lf) is a bi-lobed, iron-binding protein found on mucosal surfaces and at sites of inflammation. Gram-negative pathogens from the Neisseriaceae and Moraxellaceae families are capable of using Lf as a source of iron for growth through a process mediated by a bacterial surface receptor that directly binds host Lf. This receptor consists of an integral outer membrane protein, lactoferrin binding protein A (LbpA), and a surface lipoprotein, lactoferrin binding protein B (LbpB). The N-lobe of the homologous transferrin binding protein B, TbpB, has been shown to facilitate transferrin binding in the process of iron acquisition. Currently there is little known about the role of LbpB in iron acquisition or how Lf interacts with the bacterial receptor proteins. No structural information on any LbpB or domain is available. In this study, we express and purify from Escherichia coli the full-length LbpB and the N-lobe of LbpB from the bovine pathogen Moraxella bovis for crystallization trials. We demonstrate that M. bovis LbpB binds to bovine but not human Lf. We also report the crystal structure of the N-terminal lobe of LbpB from M. bovis and compare it with the published structures of TbpB to speculate on the process of Lf mediated iron acquisition.

PubMed: 22332934
DOI: 10.1139/o11-078

実験手法

X-RAY DIFFRACTION (2.9318 Å)