1J5L

NMR STRUCTURE OF THE ISOLATED BETA_C DOMAIN OF LOBSTER METALLOTHIONEIN-1

「1HZQ」から置き換えられました

1J5L の概要

• エントリーDOI: 10.2210/pdb1j5l/pdb
• 関連するPDBエントリー: 1J5M
• NMR情報: BMRB: 4754
• 分子名称: METALLOTHIONEIN-1, CADMIUM ION (2 entities in total)
• 機能のキーワード: beta-domain, metalloprotein, cadmium-sulfur-cluster, metal binding protein
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3470.96

構造登録者

Munoz, A.,Forsterling, F.H.,Shaw III, C.F.,Petering, D.H. (登録日: 2002-05-16, 公開日: 2002-05-22, 最終更新日: 2024-05-08)

主引用文献

Munoz, A.,Forsterling, F.H.,Shaw III, C.F.,Petering, D.H.
Structure of the (113)Cd(3)beta domains from Homarus americanus metallothionein-1: hydrogen bonding and solvent accessibility of sulfur atoms
J.Biol.Inorg.Chem., 7:713-724, 2002

PubMed Abstract: The three-dimensional structures of the isolated Cd(3)beta domains from Homarus americanus metallothionein have been determined by NMR methods in order to establish a set of beta-domain structures for comparative analysis. First, it was determined that the Cd-cysteine connectivities forming the Cd(3)S(9) metal center were identical to those observed for the beta(N) domain in the native holoprotein. Time- and temperature-dependence studies of the (113)Cd and (1)H 1D-NMR spectra indicated that the beta(N) domain undergoes slow conformational changes before reaching an equilibrium structure. In addition to structural information provided by the metal-to-cysteine connectivities, Phi, chi(1) and chi(2) angle constraints, three H(N...)S hydrogen bond interactions were also determined from a long-range optimized (1)H(N)-(113)Cd HMQC experiment. A simulated annealing protocol was applied to the distance and angle constraints obtained from the 2D-NMR experiments to calculate the three-dimensional structure of the synthetic Cd(3)beta(N) domain of lobster metallothionein. Structure-reactivity relationships are proposed for the reactions of Cd(3)beta domains with 5,5'-dithiobis(2-nitrobenzoate), based on comparisons of surface exposure of sulfur atoms of the lobster and rabbit Cd(3)beta domain structures. Finally, the surface exposure of the beta domains of lobster is compared with beta domains from mammalian metallothioneins.

PubMed: 12203008
DOI: 10.1007/s00775-002-0345-3

実験手法

SOLUTION NMR