5YY0

Crystal structure of the HyhL-HypA complex (form II)

5YY0 の概要

• エントリーDOI: 10.2210/pdb5yy0/pdb
• 分子名称: Cytosolic NiFe-hydrogenase, alpha subunit, Probable hydrogenase nickel incorporation protein HypA, ZINC ION (3 entities in total)
• 機能のキーワード: hydrogenase, maturation, hyhl, hypa, metal binding protein
• 由来する生物種: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64129.85

構造登録者

Kwon, S.,Watanabe, S.,Nishitani, Y.,Miki, K. (登録日: 2017-12-07, 公開日: 2018-06-20, 最終更新日: 2024-03-27)

主引用文献

Kwon, S.,Watanabe, S.,Nishitani, Y.,Kawashima, T.,Kanai, T.,Atomi, H.,Miki, K.
Crystal structures of a [NiFe] hydrogenase large subunit HyhL in an immature state in complex with a Ni chaperone HypA.
Proc. Natl. Acad. Sci. U.S.A., 115:7045-7050, 2018

PubMed Abstract: 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 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.

PubMed: 29915046
DOI: 10.1073/pnas.1801955115

実験手法

X-RAY DIFFRACTION (3.243 Å)