6O59

Crystal structure of the N-terminal domain of the A subunit of the Bacillus megaterium spore germinant receptor GerK3

Summary for 6O59

• Entry DOI: 10.2210/pdb6o59/pdb
• Descriptor: Germination protein (2 entities in total)
• Functional Keywords: bacillus, spores, spore germination, spore germinant recepter, transport protein
• Biological source: Bacillus megaterium
• Total number of polymer chains: 2
• Total formula weight: 60106.75

Authors

Li, Y.,Hao, B. (deposition date: 2019-03-01, release date: 2019-05-22, Last modification date: 2024-03-13)

Primary citation

Li, Y.,Jin, K.,Perez-Valdespino, A.,Federkiewicz, K.,Davis, A.,Maciejewski, M.W.,Setlow, P.,Hao, B.
Structural and functional analyses of the N-terminal domain of the A subunit of aBacillus megateriumspore germinant receptor.
Proc.Natl.Acad.Sci.USA, 116:11470-11479, 2019

PubMed Abstract: Germination of spores is induced by the interaction of specific nutrient molecules with germinant receptors (GRs) localized in the spore's inner membrane. GRs typically consist of three subunits referred to as A, B, and C, although functions of individual subunits are not known. Here we present the crystal structure of the N-terminal domain (NTD) of the A subunit of the GerK GR, revealing two distinct globular subdomains bisected by a cleft, a fold with strong homology to substrate-binding proteins in bacterial ABC transporters. Molecular docking, chemical shift perturbation measurement, and mutagenesis coupled with spore germination analyses support a proposed model that the interface between the two subdomains in the NTD of GR A subunits serves as the germinant binding site and plays a critical role in spore germination. Our findings provide a conceptual framework for understanding the germinant recruitment mechanism by which GRs trigger spore germination.

PubMed: 31113879
DOI: 10.1073/pnas.1903675116

Experimental method

X-RAY DIFFRACTION (2.79 Å)