5IV9

The LPS Transporter LptDE from Klebsiella pneumoniae, full-length

Summary for 5IV9

• Entry DOI: 10.2210/pdb5iv9/pdb
• Related: 5IV8 5IVA
• Descriptor: LPS-assembly protein LptD, LPS-assembly lipoprotein LptE, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE (3 entities in total)
• Functional Keywords: lptd, lpte, lipopolysaccharide, transporter, transport protein
• Biological source: Klebsiella pneumoniae; More
• Cellular location: Cell outer membrane : C4T9I0; Cell outer membrane ; Lipid-anchor : A0A0J4W1Y0
• Total number of polymer chains: 2
• Total formula weight: 105997.67

Authors

Botos, I.,McCarthy, J.G.,Buchanan, S.K. (deposition date: 2016-03-20, release date: 2016-05-18, Last modification date: 2024-10-16)

Primary citation

Botos, I.,Majdalani, N.,Mayclin, S.J.,McCarthy, J.G.,Lundquist, K.,Wojtowicz, D.,Barnard, T.J.,Gumbart, J.C.,Buchanan, S.K.
Structural and Functional Characterization of the LPS Transporter LptDE from Gram-Negative Pathogens.
Structure, 24:965-976, 2016

PubMed Abstract: 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 β-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° 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.

PubMed: 27161977
DOI: 10.1016/j.str.2016.03.026

Experimental method

X-RAY DIFFRACTION (4.369 Å)