2KDX

Solution structure of HypA protein

2KDX の概要

• エントリーDOI: 10.2210/pdb2kdx/pdb
• NMR情報: BMRB: 16126
• 分子名称: Hydrogenase/urease nickel incorporation protein hypA, ZINC ION (2 entities in total)
• 機能のキーワード: metallochaperone, hydrogenase, metal-binding, nickel, metal-binding protein, metal binding protein
• 由来する生物種: Helicobacter pylori (Campylobacter pylori)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13430.78

構造登録者

Xia, W.,Li, H.,Sze, K.-H. (登録日: 2009-01-20, 公開日: 2009-10-20, 最終更新日: 2024-05-15)

主引用文献

Xia, W.,Li, H.,Sze, K.-H.,Sun, H.
Structure of a nickel chaperone, HypA, from Helicobacter pylori reveals two distinct metal binding sites
J.Am.Chem.Soc., 131:10031-10040, 2009

PubMed Abstract: Metallochaperones bind metals and ensure the safe delivery of metals to the targets. They are required for the activation and maturation of nickel-containing enzymes [Ni,Fe]-hydrogenase and urease. Metallochaperone HypA was found to be essential to facilitate nickel delivery to hydrogenase together with its partner HypB, although the detailed mechanism is not clear. In this study, we have cloned hypA gene from Helicobacter pylori (strain 26695), overexpressed, and purified the protein. The zinc-bound HypA (Zn-HypA) exists as a monomer in solution, and its solution structure was determined by NMR spectroscopy together with molecular dynamics simulated annealing. Zn-HypA folds into two domains, including a zinc domain and a nickel domain with a mixed alpha/beta structure. The former houses a rigid zinc-binding site possibly with the role of structural stabilization, whereas the latter harbors a nickel-binding site at the N-terminus. Zinc binds to the four conserved cysteines tetrahedrally as evidenced by (113)Cd NMR spectroscopy, and nickel coordinates with four nitrogens of the protein probably in a square-planar geometry. Low coordination number of Ni(2+) may allow the metal to be readily transferred to its downstream receptors. Our studies may shed light on how the metallochaperone exerts its functions in intracellular nickel delivery.

PubMed: 19621959
DOI: 10.1021/ja900543y

実験手法

SOLUTION NMR