1iwn

Crystal Structure of the Outer Membrane Lipoprotein Receptor LolB Complexed with PEGMME2000

spinqualitylabelsall models 1iwn, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1iwn is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: PG5, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LOLB_ECOLI Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability.[HAMAP-Rule:MF_00233] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Crystal structures of bacterial lipoprotein localization factors, LolA and LolB.,Takeda K, Miyatake H, Yokota N, Matsuyama S, Tokuda H, Miki K EMBO J. 2003 Jul 1;22(13):3199-209. PMID:12839983 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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