4ZLH

Structure of the LapB cytoplasmic domain at 2 angstroms

Summary for 4ZLH

• Entry DOI: 10.2210/pdb4zlh/pdb
• Descriptor: Lipopolysaccharide assembly protein B, ZINC ION (3 entities in total)
• Functional Keywords: nine tpr motifs rubredoxin lipopolysaccharide regulation, metal binding protein
• Biological source: Escherichia coli O157:H7
• Total number of polymer chains: 2
• Total formula weight: 77869.70

Authors

Prince, C.C.,Jia, Z. (deposition date: 2015-05-01, release date: 2015-11-11, Last modification date: 2024-03-06)

Primary citation

Prince, C.,Jia, Z.
An Unexpected Duo: Rubredoxin Binds Nine TPR Motifs to Form LapB, an Essential Regulator of Lipopolysaccharide Synthesis.
Structure, 23:1500-1506, 2015

PubMed Abstract: Lipopolysaccharide (LPS) synthesis and export are essential pathways for bacterial growth, proliferation, and virulence. The essential protein LapB from Escherichia coli has recently been identified as a regulator of LPS synthesis. We have determined the crystal structure of LapB (without the N-terminal transmembrane helix) at 2 Å resolution using zinc single-wavelength anomalous diffraction phasing derived from a single bound zinc atom. This structure demonstrates the presence of nine tetratricopeptide repeats (TPR) motifs, including two TPR folds that were not predicted from sequence, and a rubredoxin-type metal binding domain. The rubredoxin domain is bound intimately to the TPR motifs, which has not been previously observed or predicted. Mutations in the rubredoxin/TPR interface inhibit in vivo cell growth, and in vitro studies indicate that these modifications cause local displacement of rubredoxin from its binding site without changing the secondary structure of LapB. LapB is the first reported structure to contain both a rubredoxin domain and TPR motifs.

PubMed: 26190574
DOI: 10.1016/j.str.2015.06.011

Experimental method

X-RAY DIFFRACTION (2 Å)