2MEX
Structure of the tetrameric building block of the Salmonella Typhimurium PrgI Type three secretion system needle
Summary for 2MEX
Entry DOI | 10.2210/pdb2mex/pdb |
Related | 2lpz |
NMR Information | BMRB: 18276 |
Descriptor | Protein PrgI (1 entity in total) |
Functional Keywords | secretion, needle, filament, protein transport |
Biological source | Salmonella enterica subsp. enterica serovar Typhimurium |
Total number of polymer chains | 4 |
Total formula weight | 35459.47 |
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 citation | Loquet, 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: 24328247DOI: 10.1021/ja411362q PDB entries with the same primary citation |
Experimental method | SOLID-STATE NMR |
Structure validation
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