1J5M

SOLUTION STRUCTURE OF THE SYNTHETIC 113CD_3 BETA_N DOMAIN OF LOBSTER METALLOTHIONEIN-1

Replaces:  1HZR

Summary for 1J5M

• Entry DOI: 10.2210/pdb1j5m/pdb
• Related: 1J5L
• NMR Information: BMRB: 4725
• Descriptor: METALLOTHIONEIN-1, CADMIUM ION (2 entities in total)
• Functional Keywords: metallothionein, beta-domain, metal-sulfur-cluster, 2d-nmr, 113cd-nmr, conformational changes, hn-s-hydrogen bonds, metal binding protein
• Total number of polymer chains: 1
• Total formula weight: 3184.64

Authors

Munoz, A.,Forsterling, F.H.,Shaw III, C.F.,Petering, D.H. (deposition date: 2002-05-16, release date: 2002-05-22, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

SOLUTION NMR