5iv8 | pdb_00005iv8

The LPS Transporter LptDE from Klebsiella pneumoniae, core complex

spinqualitylabelsall models 5iv8, resolution 2.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5iv8 is a 4 chain structure with sequence from "bacillus_pneumoniae"_(schroeter_1886)_flugge_1886 "bacillus pneumoniae" (schroeter 1886) flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: C8E Related: 5iva, 5iv9 Gene: AU361_02400 ("Bacillus pneumoniae" (Schroeter 1886) Flugge 1886), lptE, APU20_03225, SM74_00486, SM87_01358 ("Bacillus pneumoniae" (Schroeter 1886) Flugge 1886) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0A0J4W1Y0_KLEPN] Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.[HAMAP-Rule:MF_01186][SAAS:SAAS00074338] Publication Abstract from PubMed Incorporation of lipopolysaccharide (LPS) into the outer membrane of Gram-negative bacteria is essential for viability, and is accomplished by a two-protein complex called LptDE. We solved crystal structures of the core LptDE complexes from Yersinia pestis, Klebsiella pneumoniae, Pseudomonas aeruginosa, and a full-length structure of the K. pneumoniae LptDE complex. Our structures adopt the same plug and 26-strand beta-barrel architecture found recently for the Shigella flexneri and Salmonella typhimurium LptDE structures, illustrating a conserved fold across the family. A comparison of the only two full-length structures, SfLptDE and our KpLptDE, reveals a 21 degrees rotation of the LptD N-terminal domain that may impart flexibility on the trans-envelope LptCAD scaffold. Utilizing mutagenesis coupled to an in vivo functional assay and molecular dynamics simulations, we demonstrate the critical role of Pro231 and Pro246 in the function of the LptD lateral gate that allows partitioning of LPS into the outer membrane. Structural and Functional Characterization of the LPS Transporter LptDE from Gram-Negative Pathogens.,Botos I, Majdalani N, Mayclin SJ, McCarthy JG, Lundquist K, Wojtowicz D, Barnard TJ, Gumbart JC, Buchanan SK Structure. 2016 May 3. pii: S0969-2126(16)30043-0. doi:, 10.1016/j.str.2016.03.026. PMID:27161977 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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