4NY5

X-ray structure of the adduct formed between hen egg white lysozyme and NAMI-A

4NY5 の概要

• エントリーDOI: 10.2210/pdb4ny5/pdb
• 関連するPDBエントリー: 4J1A 4J1B
• 分子名称: Lysozyme C, RUTHENIUM ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, o-glycosyl
• 由来する生物種: Gallus gallus (bantam,chickens)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14627.20

構造登録者

Messori, L.,Merlino, A. (登録日: 2013-12-10, 公開日: 2014-03-26, 最終更新日: 2024-11-27)

主引用文献

Messori, L.,Merlino, A.
Ruthenium metalation of proteins: the X-ray structure of the complex formed between NAMI-A and hen egg white lysozyme.
Dalton Trans, 43:6128-6131, 2014

PubMed Abstract: A crystallographic study of the adduct formed between hen egg white lysozyme (HEWL) and NAMI-A, an established ruthenium(III) anticancer agent in clinical trials, is presented here. The X-ray structure reveals that NAMI-A coordinates the protein, as a naked ruthenium ion, at two distinct sites (namely Asp101 or Asp119) after releasing all its original ligands (DMSO, imidazole and Cl(-)). Structural data of the HEWL/NAMI-A adduct are compared with those previously obtained for the HEWL adduct of AziRu, a NAMI-A analogue bearing a pyridine in place of imidazole. The present results further support the view that NAMI-A exerts its biological effects acting as a classical "prodrug" first undergoing activation and then causing extensive metalation of relevant protein targets. It is also proposed that the original Ru-ligands, although absent in the final adduct, play a major role in directing the ruthenium center to its ultimate anchoring site on the protein surface.

PubMed: 24553967
DOI: 10.1039/c3dt53582g

実験手法

X-RAY DIFFRACTION (1.85 Å)