+Search query
-Structure paper
Title | A coiled-coil domain acts as a molecular ruler to regulate O-antigen chain length in lipopolysaccharide. |
---|---|
Journal, issue, pages | Nat Struct Mol Biol, Vol. 22, Issue 1, Page 50-56, Year 2015 |
Publish date | Dec 15, 2014 |
![]() | Gregor Hagelueken / Bradley R Clarke / Hexian Huang / Anne Tuukkanen / Iulia Danciu / Dmitri I Svergun / Rohanah Hussain / Huanting Liu / Chris Whitfield / James H Naismith / ![]() ![]() ![]() |
PubMed Abstract | 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 ...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. |
![]() | ![]() ![]() ![]() |
Methods | SAS (X-ray synchrotron) / X-ray diffraction |
Resolution | 3.87 Å |
Structure data | ![]() SASDAH6: ![]() SASDAJ6: ![]() PDB-4uw0: |
Chemicals | ![]() ChemComp-SAM: |
Source |
|
![]() | TRANSFERASE / KINASE / METHYLTRANSFERASE |