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Structure paper

TitleStructural Characterization of Closely Related O-antigen Lipopolysaccharide (LPS) Chain Length Regulators.
Journal, issue, pagesJ. Biol. Chem., Vol. 287, Page 15696-15705, Year 2012
Publish dateMar 7, 2012 (structure data deposition date)
AuthorsKalynych, S. / Yao, D. / Magee, J. / Cygler, M.
External linksJ. Biol. Chem. / PubMed:22437828
MethodsX-ray diffraction
Resolution1.6 - 2.8 Å
Structure data

PDB-4e29:
Periplasmic domain of the chimeric WzzB chain length regulator protein
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-4e2c:
Crystal Structure of the periplasmic domain of the chimeric LPS O-antigen chain length regulator protein
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-4e2h:
Crystal structure of the periplasmic domain of Shigella flexneri WzzB
Method: X-RAY DIFFRACTION / Resolution: 2.36 Å

PDB-4e2l:
Crystal Structure of the periplasmic domain of mutant FepE LPS O-antigen chain length regulator protein
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • shigella flexneri (bacteria)
  • salmonella typhimurium (strain lt2 / sgsc1412 / atcc 700720) (bacteria)
  • escherichia coli (E. coli)
KeywordsMEMBRANE PROTEIN / Wzz / Regulation of LPS O-antigen chain length / Inner membrane / Chimeric polysaccharide co-polymerase / Bacterial inner membrane / LPS O-antigen chain length determination / periplasmic space / FepE polysaccharride co-polymerase

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