Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Alternating L4 loop architecture of the bacterial polysaccharide co-polymerase WzzE.
Journal, issue, pages	Commun Biol, Vol. 6, Issue 1, Page 802, Year 2023
Publish date	Aug 2, 2023
Authors	Benjamin Wiseman / Göran Widmalm / Martin Högbom /
PubMed Abstract	Lipopolysaccharides such as the enterobacterial common antigen are important components of the enterobacterial cell envelope that act as a protective barrier against the environment and are often ...Lipopolysaccharides such as the enterobacterial common antigen are important components of the enterobacterial cell envelope that act as a protective barrier against the environment and are often polymerized by the inner membrane bound Wzy-dependent pathway. By employing cryo-electron microscopy we show that WzzE, the co-polymerase component of this pathway that is responsible for the length modulation of the enterobacterial common antigen, is octameric with alternating up-down conformations of its L4 loops. The alternating up-down nature of these essential loops, located at the top of the periplasmic bell, are modulated by clashing helical faces between adjacent protomers that flank the L4 loops around the octameric periplasmic bell. This alternating arrangement and a highly negatively charged binding face create a dynamic environment in which the polysaccharide chain is extended, and suggest a ratchet-type mechanism for polysaccharide elongation.
External links	Commun Biol / PubMed:37532793 / PubMed Central
Methods	EM (single particle)
Resolution	2.5 - 3.5 Å
Structure data	16071 8bhw EMDB-16071, PDB-8bhw: Full-length bacterial polysaccharide co-polymerase WzzE from E. coli. C4 symmetry Method: EM (single particle) / Resolution: 3.2 Å EMDB-16072: Full-length bacterial polysaccharide co-polymerase WzzE from E. coli. C1 symmetry Method: EM (single particle) / Resolution: 3.5 Å EMDB-16073: Full-length bacterial polysaccharide co-polymerase WzzE from E. coli. C8 symmetry Method: EM (single particle) / Resolution: 3.1 Å 17387 8p3o EMDB-17387, PDB-8p3o: Full-length bacterial polysaccharide co-polymerase WzzE mutant R267A from E. coli. C4 symmetry Method: EM (single particle) / Resolution: 2.9 Å EMDB-17388: Full-length bacterial polysaccharide co-polymerase WzzE mutant R267A from E. coli. C1 symmetry Method: EM (single particle) / Resolution: 3.1 Å 17389 8p3p EMDB-17389, PDB-8p3p: Full-length bacterial polysaccharide co-polymerase WzzE mutant R267E from E. coli. C4 symmetry Method: EM (single particle) / Resolution: 2.5 Å EMDB-17390: Full-length bacterial polysaccharide co-polymerase WzzE mutant R267E from E. coli. C1 symmetry Method: EM (single particle) / Resolution: 2.7 Å
Source	escherichia coli k-12 (bacteria)
Keywords	MEMBRANE PROTEIN / Complex / Lipopolysaccharide / bacterial polysaccharide co-polymerase