We discuss our recent results on the Escherichia coli F-ATPase, in particular its catalytic site in the beta subunit and regulation of H+ transport by the gamma subunit. Affinity labelling experiments suggest that beta Lys-155 in the glycine-rich sequence is near the gamma-phosphate moiety of ATP bound at the catalytic site. The enzyme loses activity upon introduction of missense mutations in beta Lys-155 or beta Thr-156 and changes catalytic properties upon introduction of other mutations. By analysis of mutations and their pseudo revertants, residues beta Ser-174, beta Glu-192 and beta Val-198 were found to be located near the glycine-rich sequence. The combined approaches of chemical labelling and genetics have been fruitful in visualizing the structure of the catalytic site. Analysis of mutations in the gamma subunit suggests that this subunit has an essential role in coupling catalysis with proton translocation.
Recognising our community as we approach JEB's centenary
In this Editorial, Craig Franklin, Michaela Handel and Kathryn Knight reflect on recent developments at JEB and acknowledge the support of the community during what has been a particularly challenging year. Looking forward, they discuss the journal’s centenary celebrations in 2023.
Our Transformative Journals have exceeded their OA growth targets
In the field: an interview with Roger Hanlon
Roger Hanlon talks about his fieldwork experiences diving all over the planet to understand cephalopod camouflage and communication.
How climbing parrots achieve pitch stability while ascending
Climbing parrots push and pull with their feet on ladder rungs and push with their tails to prevent themselves from toppling backward as they ascend.
Towards understanding the neural origins of hibernation
Madeleine Junkins, Sviatoslav Bagriantsev and Elena Gracheva review the role of the nervous system in hibernation, arguing that it actively promotes and supports the hibernation process rather than simply enduring it.
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