Publication Abstract from PubMed
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 alpha-helical and lipoyl domains, but not the area where it interacts with LipB, suggesting that the region is flexible without LipB. The long alpha-helical domain has three alpha-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.
Structural Basis for the Serratia marcescens Lipase Secretion System: Crystal Structures of the Membrane Fusion Protein and Nucleotide-Binding Domain.,Murata D, Okano H, Angkawidjaja C, Akutsu M, Tanaka SI, Kitahara K, Yoshizawa T, Matsumura H, Kado Y, Mizohata E, Inoue T, Sano S, Koga Y, Kanaya S, Takano K Biochemistry. 2017 Nov 10. doi: 10.1021/acs.biochem.7b00985. PMID:29094929[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
