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2MEX

Structure of the tetrameric building block of the Salmonella Typhimurium PrgI Type three secretion system needle

Summary for 2MEX
Entry DOI10.2210/pdb2mex/pdb
Related2lpz
NMR InformationBMRB: 18276
DescriptorProtein PrgI (1 entity in total)
Functional Keywordssecretion, needle, filament, protein transport
Biological sourceSalmonella enterica subsp. enterica serovar Typhimurium
Total number of polymer chains4
Total formula weight35459.47
Authors
Loquet, A.,Habenstein, B.,Chevelkov, V.,Giller, K.,Becker, S.,Lange, A. (deposition date: 2013-10-01, release date: 2013-12-25, Last modification date: 2024-05-01)
Primary citationLoquet, A.,Habenstein, B.,Chevelkov, V.,Vasa, S.K.,Giller, K.,Becker, S.,Lange, A.
Atomic structure and handedness of the building block of a biological assembly.
J.Am.Chem.Soc., 135:19135-19138, 2013
Cited by
PubMed Abstract: Noncovalent supramolecular assemblies possess in general several unique subunit-subunit interfaces.The basic building block of such an assembly consists of several subunits and contains all unique interfaces. Atomic-resolution structures of monomeric subunits are typically accessed by crystallography or solution NMR and fitted into electron microscopy density maps. However, the structure of the intact building block in the assembled state remains unknown with this hybrid approach. Here, we present the solid-state NMR atomic structure of the building block of the type III secretion system needle. The building block structure consists of a homotetrameric subunit complex with three unique supramolecular interfaces. Side-chain positions at the interfaces were solved at atomic detail. The high-resolution structure reveals unambiguously the helical handedness of the assembly, determined to be right-handed for the type III secretion system needle.Additionally, the axial rise per subunit could be extracted from the tetramer structure and independently validated by mass-per-length measurements.
PubMed: 24328247
DOI: 10.1021/ja411362q
PDB entries with the same primary citation
Experimental method
SOLID-STATE NMR
Structure validation

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數據於2024-11-06公開中

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