3VZU

Crystal Structure of outer membrane protein PorB from Neisseria meningitidis in complex with AMP-PNP

「3A2U」から置き換えられました

3VZU の概要

• エントリーDOI: 10.2210/pdb3vzu/pdb
• 関連するPDBエントリー: 3VZT 3VZW
• 分子名称: outer membrane protein, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (2 entities in total)
• 機能のキーワード: beta-barrel, porin, channel, outer membrane protein, transport, membrane protein
• 由来する生物種: Neisseria meningitidis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38685.50

構造登録者

Tanabe, M.,Iverson, T.M. (登録日: 2012-10-15, 公開日: 2013-03-13, 最終更新日: 2023-11-08)

主引用文献

Tanabe, M.,Nimigean, C.M.,Iverson, T.M.
Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB.
Proc.Natl.Acad.Sci.USA, 107:6811-6816, 2010

PubMed Abstract: PorB is the second most prevalent outer membrane protein in Neisseria meningitidis. PorB is required for neisserial pathogenesis and can elicit a Toll-like receptor mediated host immune response. Here, the x-ray crystal structure of PorB has been determined to 2.3 A resolution. Structural analysis and cocrystallization studies identify three putative solute translocation pathways through the channel pore: One pathway transports anions nonselectively, one transports cations nonselectively, and one facilitates the specific uptake of sugars. During infection, PorB likely binds host mitochondrial ATP, and cocrystallization with the ATP analog AMP-PNP suggests that binding of nucleotides regulates these translocation pathways both by partial occlusion of the pore and by restricting the motion of a putative voltage gating loop. PorB is located on the surface of N. meningitidis and can be recognized by receptors of the host innate immune system. Features of PorB suggest that Toll-like receptor mediated recognition outer membrane proteins may be initiated with a nonspecific electrostatic attraction.

PubMed: 20351243
DOI: 10.1073/pnas.0912115107

実験手法

X-RAY DIFFRACTION (2.9 Å)