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8T53

S. enterica WbaP in a styrene maleic acid liponanoparticle

Summary for 8T53
Entry DOI10.2210/pdb8t53/pdb
EMDB information41042
DescriptorUndecaprenyl-phosphate galactose phosphotransferase (1 entity in total)
Functional Keywordsphosphoglycosyl transferase, liponanopaticle, smalp, o-antigen, salmonella enterica, transferase
Biological sourceSalmonella enterica subsp. enterica serovar Typhimurium
Total number of polymer chains2
Total formula weight122765.40
Authors
Dodge, G.J.,Imperiali, B. (deposition date: 2023-06-12, release date: 2024-02-14, Last modification date: 2024-02-28)
Primary citationDodge, G.J.,Anderson, A.J.,He, Y.,Liu, W.,Viner, R.,Imperiali, B.
Mapping the architecture of the initiating phosphoglycosyl transferase from S. enterica O-antigen biosynthesis in a liponanoparticle.
Elife, 12:-, 2024
Cited by
PubMed Abstract: Bacterial cell surface glycoconjugates are critical for cell survival and for interactions between bacteria and their hosts. Consequently, the pathways responsible for their biosynthesis have untapped potential as therapeutic targets. The localization of many glycoconjugate biosynthesis enzymes to the membrane represents a significant challenge for expressing, purifying, and characterizing these enzymes. Here, we leverage cutting-edge detergent-free methods to stabilize, purify, and structurally characterize WbaP, a phosphoglycosyl transferase (PGT) from the (LT2) O-antigen biosynthesis. From a functional perspective, these studies establish WbaP as a homodimer, reveal the structural elements responsible for dimerization, shed light on the regulatory role of a domain of unknown function embedded within WbaP, and identify conserved structural motifs between PGTs and functionally unrelated UDP-sugar dehydratases. From a technological perspective, the strategy developed here is generalizable and provides a toolkit for studying other classes of small membrane proteins embedded in liponanoparticles beyond PGTs.
PubMed: 38358918
DOI: 10.7554/eLife.91125
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.1 Å)
Structure validation

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