PDBsum entry 5iv8

Transport protein

PDB id: 5iv8

Contents

Protein chains

552 a.a.

146 a.a.

Ligands

C8E ×8

Waters ×2

PDB id:

5iv8

Name:

Transport protein

Title:

The lps transporter lptde from klebsiella pneumoniae, core complex

Structure:

Lps biosynthesis protein. Chain: a, c. Fragment: unp residues 203-782. Engineered: yes. Lps-assembly lipoprotein lpte. Chain: b, d. Fragment: unp residues 20-196. Engineered: yes

Source:

Klebsiella pneumoniae. Organism_taxid: 573. Gene: au361_02400. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: lpte, apu20_03225, sm74_00486, sm87_01358.

Resolution:

2.94Å R-factor: 0.238 R-free: 0.284

Authors:

I.Botos,J.G.Mccarthy,S.K.Buchanan

Key ref:

I.Botos et al. (2016). Structural and Functional Characterization of the LPS Transporter LptDE from Gram-Negative Pathogens. Structure, 24, 965-976. PubMed id: 27161977 DOI: 10.1016/j.str.2016.03.026

Date:

20-Mar-16 Release date: 18-May-16

Protein chains

C4T9I0  (C4T9I0_KLEPN) -  LPS-assembly protein LptD from Klebsiella pneumoniae

Seq: 782 a.a.

Struc: 552 a.a.

Protein chains

A0A0J4W1Y0  (A0A0J4W1Y0_KLEVA) -  LPS-assembly lipoprotein LptE from Klebsiella variicola

Seq: 196 a.a.

Struc: 146 a.a.

DOI no: 10.1016/j.str.2016.03.026

Structure 24:965-976 (2016)

PubMed id: 27161977

Structural and Functional Characterization of the LPS Transporter LptDE from Gram-Negative Pathogens.

I.Botos, N.Majdalani, S.J.Mayclin, J.G.McCarthy, K.Lundquist, D.Wojtowicz, T.J.Barnard, J.C.Gumbart, S.K.Buchanan.

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.