5NEN

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

Summary for 5NEN

• Entry DOI: 10.2210/pdb5nen/pdb
• Descriptor: Lipase C (1 entity in total)
• Functional Keywords: lipase, hydrolase
• Biological source: Serratia marcescens
• Total number of polymer chains: 2
• Total formula weight: 99850.23

Authors

Murata, D.,Akutsu, M.,Takano, K. (deposition date: 2017-03-11, release date: 2017-11-22, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.901 Å)