2018年6月18日
Crystal structures of a [NiFe] hydrogenase large subunit HyhL in an immature state in complex with a Ni chaperone HypA.
Proceedings of the National Academy of Sciences of the United States of America
- 巻
- 115
- 号
- 27
- 開始ページ
- 7045
- 終了ページ
- 7050
- 記述言語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1073/pnas.1801955115
- 出版者・発行元
- Proceedings of the National Academy of Sciences
Ni-Fe clusters are inserted into the large subunit of [NiFe] hydrogenases by maturation proteins such as the Ni chaperone HypA via an unknown mechanism. We determined crystal structures of an immature large subunit HyhL complexed with HypA from <italic>Thermococcus kodakarensis</italic>. Structure analysis revealed that the N-terminal region of HyhL extends outwards and interacts with the Ni-binding domain of HypA. Intriguingly, the C-terminal extension of immature HyhL, which is cleaved in the mature form, adopts a β-strand adjacent to its N-terminal β-strands. The position of the C-terminal extension corresponds to that of the N-terminal extension of a mature large subunit, preventing the access of endopeptidases to the cleavage site of HyhL. These findings suggest that Ni insertion into the active site induces spatial rearrangement of both the N- and C-terminal tails of HyhL, which function as a key checkpoint for the completion of the Ni-Fe cluster assembly.
- リンク情報
- ID情報
-
- DOI : 10.1073/pnas.1801955115
- ISSN : 0027-8424
- eISSN : 1091-6490
- ORCIDのPut Code : 66645324
- PubMed ID : 29915046
- PubMed Central 記事ID : PMC6142260