期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 66, 期 -, 页码 119-128出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2020.10.027
关键词
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资金
- European Union's Horizon 2020 research and innovation programme [647784]
- CEA
- long-term EMBO fellowship [ALTF441-2017]
- Marie Sklodowska-Curie actions Individual Fellowship [789385]
- European Research Council (ERC) [647784] Funding Source: European Research Council (ERC)
- Marie Curie Actions (MSCA) [789385] Funding Source: Marie Curie Actions (MSCA)
AAA+ ATPases are a diverse protein superfamily that drive various cellular processes. Advances in cryo-EM have provided more detailed insights into their structures, leading to a better understanding of their functional relationships and revealing discrepancies in their classification.
AAA+ ATPases are a diverse protein superfamily which power a vast number of cellular processes, from protein degradation to genome replication and ribosome biogenesis. The latest advances in cryo-EM have resulted in a spectacular increase in the number and quality of AAA+ ATPase structures. This abundance of new information enables closer examination of different types of structural insertions into the conserved core, revealing discrepancies in the current classification of AAA+ modules into clades. Additionally, combined with biochemical data, it has allowed rapid progress in our understanding of structure-functional relationships and provided arguments both in favour and against the existence of a unifying molecular mechanism for the ATPase activity and action on substrates, stimulating further intensive research.
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