5ICQ

Methanobactin periplasmic binding protein

5ICQ の概要

• エントリーDOI: 10.2210/pdb5icq/pdb
• 分子名称: Methylocystis parvus OBBP MbnE, SULFATE ION (3 entities in total)
• 機能のキーワード: periplasmic binding protein, methanobactin
• 由来する生物種: Methylocystis parvus OBBP
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 68627.92

構造登録者

Dassama, L.M.K.,Rosenzweig, A.C. (登録日: 2016-02-23, 公開日: 2016-10-26, 最終更新日: 2023-09-27)

主引用文献

Dassama, L.M.,Kenney, G.E.,Ro, S.Y.,Zielazinski, E.L.,Rosenzweig, A.C.
Methanobactin transport machinery.
Proc.Natl.Acad.Sci.USA, 113:13027-13032, 2016

PubMed Abstract: Methanotrophic bacteria use methane, a potent greenhouse gas, as their primary source of carbon and energy. The first step in methane metabolism is its oxidation to methanol. In almost all methanotrophs, this chemically challenging reaction is catalyzed by particulate methane monooxygenase (pMMO), a copper-dependent integral membrane enzyme. Methanotrophs acquire copper (Cu) for pMMO by secreting a small ribosomally produced, posttranslationally modified natural product called methanobactin (Mbn). Mbn chelates Cu with high affinity, and the Cu-loaded form (CuMbn) is reinternalized into the cell via an active transport process. Bioinformatic and gene regulation studies suggest that two proteins might play a role in CuMbn handling: the TonB-dependent transporter MbnT and the periplasmic binding protein MbnE. Disruption of the gene that encodes MbnT abolishes CuMbn uptake, as reported previously, and expression of MbnT in Escherichia coli confers the ability to take up CuMbn. Biophysical studies of MbnT and MbnE reveal specific interactions with CuMbn, and a crystal structure of apo MbnE is consistent with MbnE's proposed role as a periplasmic CuMbn transporter. Notably, MbnT and MbnE exhibit different levels of discrimination between cognate and noncognate CuMbns. These findings provide evidence for CuMbn-protein interactions and begin to elucidate the molecular mechanisms of its recognition and transport.

PubMed: 27807137
DOI: 10.1073/pnas.1603578113

実験手法

X-RAY DIFFRACTION (1.9 Å)