3wjt

Crystal structure of the L68D variant of mLolB

spinqualitylabelsall models 3wjt, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wjt is a 1 chain structure with sequence from Ecod1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, SO4 Related: 3wjv, 3wju Gene: lolB, ECDH1ME8569_1148 (ECOD1) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [C9QXY7_ECOD1] Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein (By similarity).[SAAS:SAAS004565_004_010951][HAMAP-Rule:MF_00233] Publication Abstract from PubMed The Lol system comprising five Lol proteins, LolA through LolE, sorts Escherichia coli lipoproteins to outer membranes. The LolCDE complex, an ATP binding cassette transporter in inner membranes, releases outer membrane-specific lipoproteins in an ATP-dependent manner, causing formation of the LolA-lipoprotein complex in the periplasm. LolA transports lipoproteins through the periplasm to LolB on outer membranes. LolB is itself a lipoprotein anchored to outer membranes, although the membrane anchor is functionally dispensable. LolB then localizes lipoproteins to outer membranes through largely unknown mechanisms. The crystal structure of LolB is similar to that of LolA, and it possesses a hydrophobic cavity that accommodates acyl chains of lipoproteins. To elucidate the molecular function of LolB, a periplasmic version of LolB, mLolB, was mutagenized at various conserved residues. Despite the lack of acyl chains, most defective mutants were insoluble. However, a derivative with glutamate in place of leucine 68 was soluble and unable to localize lipoproteins to outer membranes. This leucine is present in a loop protruding from mLolB into an aqueous environment, and no analogous loop is present in LolA. Thus, leucine 68 was replaced with other residues. Replacement by acidic, but not hydrophobic, residues generated for the first time mLolB derivatives that can accept but cannot localize lipoproteins to outer membranes. Moreover, deletion of the leucine with neighboring residues impaired the lipoprotein receptor activity. Based on these observations, the roles of the protruding loop of LolB in the last step of lipoprotein sorting are discussed. Roles of the Protruding Loop of Factor B Essential for the Localization of Lipoproteins (LolB) in the Anchoring of Bacterial Triacylated Proteins to the Outer Membrane.,Hayashi Y, Tsurumizu R, Tsukahara J, Takeda K, Narita S, Mori M, Miki K, Tokuda H J Biol Chem. 2014 Apr 11;289(15):10530-9. doi: 10.1074/jbc.M113.539270. Epub 2014, Feb 25. PMID:24569999 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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