5NEN

Crystal structure of the soluble domain of LipC, a membrane fusion protein of a type I secretion system

5NEN の概要

• エントリーDOI: 10.2210/pdb5nen/pdb
• 分子名称: Lipase C (1 entity in total)
• 機能のキーワード: lipase, hydrolase
• 由来する生物種: Serratia marcescens
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 99850.23

構造登録者

Murata, D.,Akutsu, M.,Takano, K. (登録日: 2017-03-11, 公開日: 2017-11-22, 最終更新日: 2024-05-08)

主引用文献

Murata, D.,Okano, H.,Angkawidjaja, C.,Akutsu, M.,Tanaka, S.I.,Kitahara, K.,Yoshizawa, T.,Matsumura, H.,Kado, Y.,Mizohata, E.,Inoue, T.,Sano, S.,Koga, Y.,Kanaya, S.,Takano, K.
Structural Basis for the Serratia marcescens Lipase Secretion System: Crystal Structures of the Membrane Fusion Protein and Nucleotide-Binding Domain.
Biochemistry, 56:6281-6291, 2017

PubMed Abstract: Serratia marcescens secretes a lipase, LipA, through a type I secretion system (T1SS). The T1SS for LipA, the Lip system, is composed of an inner membrane ABC transporter with its nucleotide-binding domains (NBD), LipB, a membrane fusion protein, LipC, and an outer membrane channel protein, LipD. Passenger protein secreted by this system has been functionally and structurally characterized well, but relatively little information about the transporter complex is available. Here, we report the crystallographic studies of LipC without the membrane anchor region, LipC-, and the NBD of LipB (LipB-NBD). LipC- crystallographic analysis has led to the determination of the structure of the long α-helical and lipoyl domains, but not the area where it interacts with LipB, suggesting that the region is flexible without LipB. The long α-helical domain has three α-helices, which interacts with LipD in the periplasm. LipB-NBD has the common overall architecture and ATP hydrolysis activity of ABC transporter NBDs. Using the predicted models of full-length LipB and LipD, the overall structural insight into the Lip system is discussed.

PubMed: 29094929
DOI: 10.1021/acs.biochem.7b00985

実験手法

X-RAY DIFFRACTION (2.901 Å)