9UP5

Crystal structure of LapB from Klebsiella pneumoniae

Summary for 9UP5

• Entry DOI: 10.2210/pdb9up5/pdb
• Descriptor: Lipopolysaccharide assembly protein B (1 entity in total)
• Functional Keywords: lipopolysaccharide assembly, protein-protein interaction, inner membrane protein, envelope biogenesis, chaperone
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 2
• Total formula weight: 77614.57

Authors

Jung, K.H.,Lee, S.Y.,Park, H.H. (deposition date: 2025-04-27, release date: 2026-03-04)

Primary citation

Jung, K.H.,Lee, S.Y.,Park, S.E.,Kang, Y.W.,Park, H.H.
Structural analysis of LabB from Klebsiella pneumoniae reveals an alternative dimeric conformation generated by the sliding of TPR motifs.
Biochem.Biophys.Res.Commun., 775:152151-152151, 2025

PubMed Abstract: LabB (YciM) is a key regulator of lipopolysaccharide (LPS) biosynthesis in Gram-negative bacteria, modulating LpxC degradation to maintain outer membrane integrity. While E. coli LabB (ecLabB) forms a closed-ring dimer via TPR motifs, the crystal structure of Klebsiella pneumoniae LabB (kpLabB) reveals a distinct open-ring dimeric architecture, generated by TPR motif sliding. This alternative conformation suggests a potential mechanism for dynamic regulation and partner interactions.

PubMed: 40480088
DOI: 10.1016/j.bbrc.2025.152151

Experimental method

X-RAY DIFFRACTION (3.44 Å)