Document Type

Article

Disciplines

Life Sciences | Medicine and Health Sciences

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 Å resolution. The GerBC protein adopts a previously uncharacterized type of protein fold consisting of three distinct domains, each of which is centered by a β sheet surrounded by multiple α 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.

Comments

J Mol Biol. Author manuscript; available in PMC 2013 March 26. Published in final edited form as: J Mol Biol. 2010 September 10; 402(1): 8–16. Published online 2010 July 21. doi: 10.1016/j.jmb.2010.07.018 PMCID: PMC3607951 NIHMSID: NIHMS451709

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