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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Nat+Struct+Mol+Biol
2015 ; 22
(1
): 50-56
Nephropedia Template TP
gab.com Text
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English Wikipedia
A coiled-coil domain acts as a molecular ruler to regulate O-antigen chain length
in lipopolysaccharide
#MMPMID25504321
Hagelueken G
; Clarke BR
; Huang H
; Tuukkanen A
; Danciu I
; Svergun DI
; Hussain R
; Liu H
; Whitfield C
; Naismith JH
Nat Struct Mol Biol
2015[Jan]; 22
(1
): 50-56
PMID25504321
show ga
Long-chain bacterial polysaccharides have important roles in pathogenicity. In
Escherichia coli O9a, a model for ABC transporter-dependent polysaccharide
assembly, a large extracellular carbohydrate with a narrow size distribution is
polymerized from monosaccharides by a complex of two proteins, WbdA (polymerase)
and WbdD (terminating protein). Combining crystallography and small-angle X-ray
scattering, we found that the C-terminal domain of WbdD contains an extended
coiled-coil that physically separates WbdA from the catalytic domain of WbdD. The
effects of insertions and deletions in the coiled-coil region were analyzed in
vivo, revealing that polymer size is controlled by varying the length of the
coiled-coil domain. Thus, the coiled-coil domain of WbdD functions as a molecular
ruler that, along with WbdA:WbdD stoichiometry, controls the chain length of a
model bacterial polysaccharide.