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PDBsum entry 4zm5
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Membrane protein
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PDB id
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4zm5
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PDB id:
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| Name: |
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Membrane protein
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Title:
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Shigella flexneri lipopolysaccharide o-antigen chain-length regulator wzzbsf - a107p mutant
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Structure:
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Chain length determinant protein. Chain: a, b, c. Fragment: unp residues 54-293. Synonym: polysaccharide antigen chain regulator. Engineered: yes. Mutation: yes
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Source:
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Shigella flexneri. Organism_taxid: 623. Strain: rma4053. Variant: serotype y wzz::kanr. Gene: wzzb, cld, rol, sf2089, s2210. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.47Å
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R-factor:
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0.198
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R-free:
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0.242
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Authors:
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D.J.Ericsson,C.-W.Chang,T.Lonhienne,L.Casey,F.Benning,B.Kobe, E.N.H.Tran,R.Morona
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Key ref:
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C.W.Chang
et al.
(2015).
Structural and Biochemical Analysis of a Single Amino-Acid Mutant of WzzBSF That Alters Lipopolysaccharide O-Antigen Chain Length in Shigella flexneri.
Plos One,
10,
e0138266.
PubMed id:
DOI:
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Date:
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02-May-15
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Release date:
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23-Mar-16
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PROCHECK
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Headers
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References
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P37792
(WZZB_SHIFL) -
Chain length determinant protein from Shigella flexneri
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Seq:
Struc:
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325 a.a.
230 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Plos One
10:e0138266
(2015)
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PubMed id:
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Structural and Biochemical Analysis of a Single Amino-Acid Mutant of WzzBSF That Alters Lipopolysaccharide O-Antigen Chain Length in Shigella flexneri.
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C.W.Chang,
E.N.Tran,
D.J.Ericsson,
L.W.Casey,
T.Lonhienne,
F.Benning,
R.Morona,
B.Kobe.
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ABSTRACT
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Lipopolysaccharide (LPS), a surface polymer of Gram-negative bacteria, helps
bacteria survive in different environments and acts as a virulence determinant
of host infection. The O-antigen (Oag) component of LPS exhibits a modal
chain-length distribution that is controlled by polysaccharide co-polymerases
(PCPs). The molecular basis of the regulation of Oag chain-lengths remains
unclear, despite extensive mutagenesis and structural studies of PCPs from
Escherichia coli and Shigella. Here, we identified a single mutation (A107P) of
the Shigella flexneri WzzBSF, by a random mutagenesis approach, that causes a
shortened Oag chain-length distribution in bacteria. We determined the crystal
structures of the periplasmic domains of wild-type WzzBSF and the A107P mutant.
Both structures form a highly similar open trimeric assembly in the crystals,
and show a similar tendency to self-associate in solution. Binding studies by
bio-layer interferometry reveal cooperative binding of very short
(VS)-core-plus-O-antigen polysaccharide (COPS) to the periplasmic domains of
both proteins, but with decreased affinity for the A107P mutant. Our studies
reveal that subtle and localized structural differences in PCPs can have
dramatic effects on LPS chain-length distribution in bacteria, for example by
altering the affinity for the substrate, which supports the role of the
structure of the growing Oag polymer in this process.
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Links
