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8TSL

S. thermodepolymerans KpsM-KpsE in Apo 2 state with rigid body fitted KpsT

Summary for 8TSL
Entry DOI10.2210/pdb8tsl/pdb
EMDB information41595
DescriptorTransport permease protein, Capsular biosynthesis protein, ABC transporter ATP-binding protein (3 entities in total)
Functional Keywordsabc transporter, capsular polysaccharide, membrane protein
Biological sourceCaldimonas thermodepolymerans
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Total number of polymer chains12
Total formula weight466509.50
Authors
Kuklewicz, J.,Zimmer, J. (deposition date: 2023-08-11, release date: 2024-04-17, Last modification date: 2024-11-06)
Primary citationKuklewicz, J.,Zimmer, J.
Molecular insights into capsular polysaccharide secretion.
Nature, 628:901-909, 2024
Cited by
PubMed Abstract: Capsular polysaccharides (CPSs) fortify the cell boundaries of many commensal and pathogenic bacteria. Through the ABC-transporter-dependent biosynthesis pathway, CPSs are synthesized intracellularly on a lipid anchor and secreted across the cell envelope by the KpsMT ABC transporter associated with the KpsE and KpsD subunits. Here we use structural and functional studies to uncover crucial steps of CPS secretion in Gram-negative bacteria. We show that KpsMT has broad substrate specificity and is sufficient for the translocation of CPSs across the inner bacterial membrane, and we determine the cell surface organization and localization of CPSs using super-resolution fluorescence microscopy. Cryo-electron microscopy analyses of the KpsMT-KpsE complex in six different states reveal a KpsE-encaged ABC transporter, rigid-body conformational rearrangements of KpsMT during ATP hydrolysis and recognition of a glycolipid inside a membrane-exposed electropositive canyon. In vivo CPS secretion assays underscore the functional importance of canyon-lining basic residues. Combined, our analyses suggest a molecular model of CPS secretion by ABC transporters.
PubMed: 38570679
DOI: 10.1038/s41586-024-07248-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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PDB entries from 2024-11-13

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