Crystal structure of E. coli lipoprotein diacylglyceryl transferase

Lipoprotein biogenesis is essential for bacterial survival. Phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (Lgt) is an integral membrane enzyme that catalyses the first reaction of the three-step post-translational lipid modification. Deletion of the lgt gene is lethal to most Gram-n...

Full description

Bibliographic Details
Main Authors:	Mao, Guotao, Zhao, Yan, Kang, Xusheng, Li, Zhijie, Zhang, Yan, Wang, Xianping, Sun, Fei, Sankaran, Krishnan, Zhang, Xuejun C.
Format:	Online
Language:	English
Published:	Nature Publishing Group 2016
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4728403/

id	pubmed-4728403
recordtype	oai_dc
spelling	pubmed-47284032016-03-04 Crystal structure of E. coli lipoprotein diacylglyceryl transferase Mao, Guotao Zhao, Yan Kang, Xusheng Li, Zhijie Zhang, Yan Wang, Xianping Sun, Fei Sankaran, Krishnan Zhang, Xuejun C. Article Lipoprotein biogenesis is essential for bacterial survival. Phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (Lgt) is an integral membrane enzyme that catalyses the first reaction of the three-step post-translational lipid modification. Deletion of the lgt gene is lethal to most Gram-negative bacteria. Here we present the crystal structures of Escherichia coli Lgt in complex with phosphatidylglycerol and the inhibitor palmitic acid at 1.9 and 1.6 Å resolution, respectively. The structures reveal the presence of two binding sites and support the previously reported structure–function relationships of Lgt. Complementation results of lgt-knockout cells with different mutant Lgt variants revealed critical residues, including Arg143 and Arg239, that are essential for diacylglyceryl transfer. Using a GFP-based in vitro assay, we correlated the activities of Lgt with structural observations. Together, the structural and biochemical data support a mechanism whereby substrate and product, lipid-modified lipobox-containing peptide, enter and leave the enzyme laterally relative to the lipid bilayer. Nature Publishing Group 2016-01-05 /pmc/articles/PMC4728403/ /pubmed/26729647 http://dx.doi.org/10.1038/ncomms10198 Text en Copyright © 2016, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Mao, Guotao Zhao, Yan Kang, Xusheng Li, Zhijie Zhang, Yan Wang, Xianping Sun, Fei Sankaran, Krishnan Zhang, Xuejun C.
spellingShingle	Mao, Guotao Zhao, Yan Kang, Xusheng Li, Zhijie Zhang, Yan Wang, Xianping Sun, Fei Sankaran, Krishnan Zhang, Xuejun C. Crystal structure of E. coli lipoprotein diacylglyceryl transferase
author_facet	Mao, Guotao Zhao, Yan Kang, Xusheng Li, Zhijie Zhang, Yan Wang, Xianping Sun, Fei Sankaran, Krishnan Zhang, Xuejun C.
author_sort	Mao, Guotao
title	Crystal structure of E. coli lipoprotein diacylglyceryl transferase
title_short	Crystal structure of E. coli lipoprotein diacylglyceryl transferase
title_full	Crystal structure of E. coli lipoprotein diacylglyceryl transferase
title_fullStr	Crystal structure of E. coli lipoprotein diacylglyceryl transferase
title_full_unstemmed	Crystal structure of E. coli lipoprotein diacylglyceryl transferase
title_sort	crystal structure of e. coli lipoprotein diacylglyceryl transferase
description	Lipoprotein biogenesis is essential for bacterial survival. Phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (Lgt) is an integral membrane enzyme that catalyses the first reaction of the three-step post-translational lipid modification. Deletion of the lgt gene is lethal to most Gram-negative bacteria. Here we present the crystal structures of Escherichia coli Lgt in complex with phosphatidylglycerol and the inhibitor palmitic acid at 1.9 and 1.6 Å resolution, respectively. The structures reveal the presence of two binding sites and support the previously reported structure–function relationships of Lgt. Complementation results of lgt-knockout cells with different mutant Lgt variants revealed critical residues, including Arg143 and Arg239, that are essential for diacylglyceryl transfer. Using a GFP-based in vitro assay, we correlated the activities of Lgt with structural observations. Together, the structural and biochemical data support a mechanism whereby substrate and product, lipid-modified lipobox-containing peptide, enter and leave the enzyme laterally relative to the lipid bilayer.
publisher	Nature Publishing Group
publishDate	2016
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4728403/
_version_	1613528979422052352

Crystal structure of E. coli lipoprotein diacylglyceryl transferase

Similar Items