4UW0
Low resolution structure of WbdD with C-terminal bundle ordered to residue 505
Summary for 4UW0
| Entry DOI | 10.2210/pdb4uw0/pdb |
| Descriptor | WBDD, S-ADENOSYLMETHIONINE (2 entities in total) |
| Functional Keywords | transferase, kinase, methyltransferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 58143.51 |
| Authors | Hagelueken, G.,Huang, H.,Naismith, J.H. (deposition date: 2014-08-08, release date: 2014-08-27, Last modification date: 2024-05-08) |
| Primary citation | Hagelueken, G.,Clarke, B.R.,Huang, H.,Tuukkanen, A.,Danciu, I.,Svergun, D.I.,Hussain, R.,Liu, H.,Whitfield, C.,Naismith, J.H. A Coiled-Coil Domain Acts as a Molecular Ruler to Regulate O-Antigen Chain Length in Lipopolysaccharide. Nat.Struct.Mol.Biol., 22:50-, 2015 Cited by 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 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. PubMed: 25504321DOI: 10.1038/NSMB.2935 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.87 Å) |
Structure validation
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