Structural highlights
FunctionYJOB_BACSU Shows ATPase activity.[1] Publication Abstract from PubMedAAA+ ATPases are ubiquitous proteins associated with most cellular processes, including DNA unwinding and protein unfolding. Their functional and structural properties are typically determined by domains and motifs added to the conserved ATPases domain. Currently, the molecular function and structure of many ATPases remain elusive. Here, we report the crystal structure and biochemical analyses of YjoB, a Bacillus subtilis AAA+ protein. The crystal structure revealed that the YjoB hexamer forms a bucket hat-shaped structure with a porous chamber. Biochemical analyses showed that YjoB prevents the aggregation of vegetative catalase KatA and gluconeogenesis-specific glyceraldehyde-3 phosphate dehydrogenase GapB but not citrate synthase, a conventional substrate. Structural and biochemical analyses further showed that the internal chamber of YjoB is necessary for inhibition of substrate aggregation. Our results suggest that YjoB, conserved in the class Bacilli, is a potential molecular chaperone acting in the starvation/stationary phases of B. subtilis growth. Crystal structure and biochemical analysis suggest that YjoB ATPase is a putative substrate-specific molecular chaperone.,Kwon E, Dahal P, Kim DY Proc Natl Acad Sci U S A. 2022 Oct 11;119(41):e2207856119. doi:, 10.1073/pnas.2207856119. Epub 2022 Oct 3. PMID:36191235[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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