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PDBsum entry 4zlh
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Metal binding protein
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PDB id
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4zlh
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References listed in PDB file
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Key reference
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Title
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An unexpected duo: rubredoxin binds nine tpr motifs to form lapb, An essential regulator of lipopolysaccharide synthesis.
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Authors
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C.Prince,
Z.Jia.
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Ref.
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Structure, 2015,
23,
1500-1506.
[DOI no: ]
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PubMed id
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Abstract
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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.
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