3N54
Crystal Structure of the GerBC protein
Summary for 3N54
| Entry DOI | 10.2210/pdb3n54/pdb |
| Descriptor | Spore germination protein B3, SULFATE ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | a novel fold, lipid binding protein |
| Biological source | Bacillus subtilis subsp. subtilis |
| Cellular location | Cell membrane; Lipid-anchor (Probable): P39571 |
| Total number of polymer chains | 1 |
| Total formula weight | 40971.68 |
| Authors | Li, Y.,Setlow, B.,Setlow, P.,Hao, B. (deposition date: 2010-05-24, release date: 2010-08-04, Last modification date: 2024-02-21) |
| Primary citation | Li, Y.,Setlow, B.,Setlow, P.,Hao, B. Crystal Structure of the GerBC Component of a Bacillus subtilis Spore Germinant Receptor. J.Mol.Biol., 402:8-16, 2010 Cited by PubMed Abstract: The nutrient germinant receptors (nGRs) of spores of Bacillus species are clusters of three proteins that play a critical role in triggering the germination of dormant spores in response to specific nutrient molecules. Here, we report the crystal structure of the C protein of the GerB germinant receptor, so-called GerBC, of Bacillus subtilis spores at 2.3 A resolution. The GerBC protein adopts a previously uncharacterized type of protein fold consisting of three distinct domains, each of which is centered by a beta sheet surrounded by multiple alpha helices. Secondary-structure prediction and structure-based sequence alignment suggest that the GerBC structure represents the prototype for C subunits of nGRs from spores of all Bacillales and Clostridiales species and defines two highly conserved structural regions in this family of proteins. GerBC forms an interlocked dimer in the crystalline state but is predominantly monomeric in solution, pointing to the possibility that GerBC oligomerizes as a result of either high local protein concentrations or interaction with other nGR proteins in spores. Our findings provide the first structural view of the nGR subunits and a molecular framework for understanding the architecture, conservation, and function of nGRs. PubMed: 20654628DOI: 10.1016/j.jmb.2010.07.018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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