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7ZE0

Solution structure of the PulM C-terminal domain from Klebsiella oxytoca

This is a non-PDB format compatible entry.
Summary for 7ZE0
Entry DOI10.2210/pdb7ze0/pdb
NMR InformationBMRB: 34719
DescriptorType II secretion system protein M (1 entity in total)
Functional Keywordsklebsiella oxytoca t2ss general secretion pathway ferredoxin-like domain, protein transport
Biological sourceKlebsiella oxytoca
Total number of polymer chains2
Total formula weight17876.33
Authors
Lopez-Castilla, A.,Bardiaux, B.,Nilges, M.,Francetic, O.,Izadi-Pruneyre, N. (deposition date: 2022-03-30, release date: 2023-01-18, Last modification date: 2024-06-19)
Primary citationDazzoni, R.,Li, Y.,Lopez-Castilla, A.,Brier, S.,Mechaly, A.,Cordier, F.,Haouz, A.,Nilges, M.,Francetic, O.,Bardiaux, B.,Izadi-Pruneyre, N.
Structure and dynamic association of an assembly platform subcomplex of the bacterial type II secretion system.
Structure, 31:152-, 2023
Cited by
PubMed Abstract: Type II secretion systems (T2SSs) allow diderm bacteria to secrete hydrolytic enzymes, adhesins, or toxins important for growth and virulence. To promote secretion of folded proteins, T2SSs assemble periplasmic filaments called pseudopili or endopili at an inner membrane subcomplex, the assembly platform (AP). Here, we combined biophysical approaches, nuclear magnetic resonance (NMR) and X-ray crystallography, to study the Klebsiella AP components PulL and PulM. We determined the structure and associations of their periplasmic domains and describe the structure of the heterodimer formed by their ferredoxin-like domains. We show how structural complementarity and plasticity favor their association during the secretion process. Cysteine scanning and crosslinking data provided additional constraints to build a structural model of the PulL-PulM assembly in the cellular context. Our structural and functional insights, together with the relative cellular abundance of its components, support the role of AP as a dynamic hub that orchestrates pilus polymerization.
PubMed: 36586404
DOI: 10.1016/j.str.2022.12.003
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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