7KYO
PsaBC from Streptococcus pneumoniae in complex with Fab
Summary for 7KYO
Entry DOI | 10.2210/pdb7kyo/pdb |
Descriptor | Manganese ABC transporter, ATP-binding protein, Fab heavy chain, Fab light chain, ... (5 entities in total) |
Functional Keywords | abc transporter manganese, transport protein-immune system complex, transport protein/immune system |
Biological source | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) More |
Total number of polymer chains | 4 |
Total formula weight | 105999.96 |
Authors | Maher, M.J.,Sjohamn, J. (deposition date: 2020-12-08, release date: 2021-08-25, Last modification date: 2024-11-13) |
Primary citation | Neville, S.L.,Sjohamn, J.,Watts, J.A.,MacDermott-Opeskin, H.,Fairweather, S.J.,Ganio, K.,Carey Hulyer, A.,McGrath, A.P.,Hayes, A.J.,Malcolm, T.R.,Davies, M.R.,Nomura, N.,Iwata, S.,O'Mara, M.L.,Maher, M.J.,McDevitt, C.A. The structural basis of bacterial manganese import. Sci Adv, 7:-, 2021 Cited by PubMed Abstract: Metal ions are essential for all forms of life. In prokaryotes, ATP-binding cassette (ABC) permeases serve as the primary import pathway for many micronutrients including the first-row transition metal manganese. However, the structural features of ionic metal transporting ABC permeases have remained undefined. Here, we present the crystal structure of the manganese transporter PsaBC from in an open-inward conformation. The type II transporter has a tightly closed transmembrane channel due to "extracellular gating" residues that prevent water permeation or ion reflux. Below these residues, the channel contains a hitherto unreported metal coordination site, which is essential for manganese translocation. Mutagenesis of the extracellular gate perturbs manganese uptake, while coordination site mutagenesis abolishes import. These structural features are highly conserved in metal-specific ABC transporters and are represented throughout the kingdoms of life. Collectively, our results define the structure of PsaBC and reveal the features required for divalent cation transport. PubMed: 34362732DOI: 10.1126/sciadv.abg3980 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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