1UA8

Crystal structure of the lipoprotein localization factor, LolA

Summary for 1UA8

• Entry DOI: 10.2210/pdb1ua8/pdb
• Related: 1IWL 1IWM 1IWN
• Descriptor: Outer-membrane lipoproteins carrier protein (2 entities in total)
• Functional Keywords: unclosed beta barrel, protein transport
• Biological source: Escherichia coli
• Cellular location: Periplasm: P61316
• Total number of polymer chains: 1
• Total formula weight: 20343.29

Authors

Takeda, K.,Miyatake, H.,Yokota, N.,Matsuyama, S.,Tokuda, H.,Miki, K. (deposition date: 2003-03-04, release date: 2003-07-15, Last modification date: 2023-10-25)

Primary citation

Takeda, K.,Miyatake, H.,Yokota, N.,Matsuyama, S.,Tokuda, H.,Miki, K.
Crystal structures of bacterial lipoprotein localization factors, LolA and LolB.
Embo J., 22:3199-3209, 2003

PubMed Abstract: Lipoproteins having a lipid-modified cysteine at the N-terminus are localized on either the inner or the outer membrane of Escherichia coli depending on the residue at position 2. Five Lol proteins involved in the sorting and membrane localization of lipoprotein are highly conserved in Gram-negative bacteria. We determined the crystal structures of a periplasmic chaperone, LolA, and an outer membrane lipoprotein receptor, LolB. Despite their dissimilar amino acid sequences, the structures of LolA and LolB are strikingly similar to each other. Both have a hydrophobic cavity consisting of an unclosed beta barrel and an alpha-helical lid. The cavity represents a possible binding site for the lipid moiety of lipoproteins. Detailed structural differences between the two proteins provide significant insights into the molecular mechanisms underlying the energy-independent transfer of lipoproteins from LolA to LolB and from LolB to the outer membrane. Furthermore, the structures of both LolA and LolB determined from different crystal forms revealed the distinct structural dynamics regarding the association and dissociation of lipoproteins. The results are discussed in the context of the current model for the lipoprotein transfer from the inner to the outer membrane through a hydrophilic environment.

PubMed: 12839983
DOI: 10.1093/emboj/cdg324

Experimental method

X-RAY DIFFRACTION (1.9 Å)