7W42

Crystal structure of Bacillus subtilis YjoB

Summary for 7W42

• Entry DOI: 10.2210/pdb7w42/pdb
• Descriptor: Uncharacterized ATPase YjoB (2 entities in total)
• Functional Keywords: aaa protein, chaperone, hydrolase
• Biological source: Bacillus subtilis (strain 168)
• Total number of polymer chains: 2
• Total formula weight: 97951.56

Authors

Dahal, P.,Kwon, E.,Kim, D.Y. (deposition date: 2021-11-26, release date: 2022-10-19, Last modification date: 2024-05-29)

Primary citation

Kwon, E.,Dahal, P.,Kim, D.Y.
Crystal structure and biochemical analysis suggest that YjoB ATPase is a putative substrate-specific molecular chaperone.
Proc.Natl.Acad.Sci.USA, 119:e2207856119-e2207856119, 2022

PubMed Abstract: AAA+ 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 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 growth.

PubMed: 36191235
DOI: 10.1073/pnas.2207856119

Experimental method

X-RAY DIFFRACTION (2.619 Å)