ISDA: 9UP5

Deposition Date 2025-04-27

Release Date 2026-03-04

Last Version Date 2026-03-04

Entry Detail

PDB ID:

9UP5

Keywords:

CHAPERONE

Title:

Crystal structure of LapB from Klebsiella pneumoniae

Biological Source:

Source Organism(s):

Klebsiella pneumoniae (Taxon ID: 573)

Expression System(s):

Escherichia coli bl21(de3)

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

3.44 Å

R-Value Free:

0.26

R-Value Work:

0.22

R-Value Observed:

0.23

Space Group:

C 1 2 1

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Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:Lipopolysaccharide assembly p
Gene (Uniprot):lapB
Chain IDs:A, B
Chain Length:338
Number of Molecules:2
Biological Source:Klebsiella pneumoniae

UniProt ID:B5XS10

Ligand Molecules

Primary Citation

Structural analysis of LabB from Klebsiella pneumoniae reveals an alternative dimeric conformation generated by the sliding of TPR motifs.

Jung, K.H, Lee, S.Y, Park, S.E, Kang, Y.W, Park, H.H.Show

Biochem.Biophys.Res.Commun. 775 152151 152151 (2025)

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

Abstact

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.

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Primary Citation of related structures

Abstact

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