8G3F
BceAB-S nucleotide free BceS state 1
Summary for 8G3F
| Entry DOI | 10.2210/pdb8g3f/pdb |
| EMDB information | 29690 29691 29694 29701 29716 29717 |
| Descriptor | Bacitracin export permease protein BceB, Bacitracin export ATP-binding protein BceA, Sensor protein BceS, ... (6 entities in total) |
| Functional Keywords | abc transporter, histidine kinase, antimicrobial, membrane protein |
| Biological source | Bacillus subtilis subsp. subtilis str. 168 More |
| Total number of polymer chains | 5 |
| Total formula weight | 210357.54 |
| Authors | George, N.L.,Orlando, B.J. (deposition date: 2023-02-07, release date: 2023-06-21, Last modification date: 2024-06-19) |
| Primary citation | George, N.L.,Orlando, B.J. Architecture of a complete Bce-type antimicrobial peptide resistance module. Nat Commun, 14:3896-3896, 2023 Cited by PubMed Abstract: Gram-positive bacteria synthesize and secrete antimicrobial peptides that target the essential process of peptidoglycan synthesis. These antimicrobial peptides not only regulate the dynamics of microbial communities but are also of clinical importance as exemplified by peptides such as bacitracin, vancomycin, and daptomycin. Many gram-positive species have evolved specialized antimicrobial peptide sensing and resistance machinery known as Bce modules. These modules are membrane protein complexes formed by an unusual Bce-type ABC transporter interacting with a two-component system sensor histidine kinase. In this work, we provide the first structural insight into how the membrane protein components of these modules assemble into a functional complex. A cryo-EM structure of an entire Bce module revealed an unexpected mechanism of complex assembly, and extensive structural flexibility in the sensor histidine kinase. Structures of the complex in the presence of a non-hydrolysable ATP analog reveal how nucleotide binding primes the complex for subsequent activation. Accompanying biochemical data demonstrate how the individual membrane protein components of the complex exert functional control over one another to create a tightly regulated enzymatic system. PubMed: 37393310DOI: 10.1038/s41467-023-39678-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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