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7KYO

PsaBC from Streptococcus pneumoniae in complex with Fab

Summary for 7KYO
Entry DOI10.2210/pdb7kyo/pdb
DescriptorManganese ABC transporter, ATP-binding protein, Fab heavy chain, Fab light chain, ... (5 entities in total)
Functional Keywordsabc transporter manganese, transport protein-immune system complex, transport protein/immune system
Biological sourceStreptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
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Total number of polymer chains4
Total formula weight105999.96
Authors
Maher, M.J.,Sjohamn, J. (deposition date: 2020-12-08, release date: 2021-08-25, Last modification date: 2024-11-13)
Primary citationNeville, 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: 34362732
DOI: 10.1126/sciadv.abg3980
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.85 Å)
Structure validation

240971

数据于2025-08-27公开中

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