PDBsum entry 2f5h

Metal binding protein

PDB id: 2f5h

Contents

Protein chain

37 a.a.

Metals

_CD ×4

PDB id:

2f5h

Name:

Metal binding protein

Title:

Solution structure of the alpha-domain of human metallothionein-3

Structure:

Metallothionein-3. Chain: a. Fragment: c-terminal (alpha) domain. Synonym: mt-3, metallothionein-iii, mt-iii, growth inhibitory factor, gif, gifb. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

NMR struc:

10 models

Authors:

H.Wang,Q.Zhang,B.Cai,H.Y.Li,K.H.Sze,Z.X.Huang,H.M.Wu,H.Z.Sun

Key ref:

H.Wang et al. (2006). Solution structure and dynamics of human metallothionein-3 (MT-3). FEBS Lett, 580, 795-800. PubMed id: 16413543 DOI: 10.1016/j.febslet.2005.12.099

Date:

25-Nov-05 Release date: 30-May-06

Protein chain

P25713  (MT3_HUMAN) -  Metallothionein-3 from Homo sapiens

Seq: 68 a.a.

Struc: 37 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.febslet.2005.12.099

FEBS Lett 580:795-800 (2006)

PubMed id: 16413543

Solution structure and dynamics of human metallothionein-3 (MT-3).

H.Wang, Q.Zhang, B.Cai, H.Li, K.H.Sze, Z.X.Huang, H.M.Wu, H.Sun.

ABSTRACT

Alzheimer's disease is characterized by progressive loss of neurons accompanied by the formation of intraneural neurofibrillary tangles and extracellular amyloid plaques. Human neuronal growth inhibitory factor, classified as metallothionein-3 (MT-3), was found to be related to the neurotrophic activity promoting cortical neuron survival and dendrite outgrowth in the cell culture studies. We have determined the solution structure of the alpha-domain of human MT-3 (residues 32-68) by multinuclear and multidimensional NMR spectroscopy in combination with the molecular dynamic simulated annealing approach. The human MT-3 shows two metal-thiolate clusters, one in the N-terminus (beta-domain) and one in the C-terminus (alpha-domain). The overall fold of the alpha-domain is similar to that of mouse MT-3. However, human MT-3 has a longer loop in the acidic hexapeptide insertion than that of mouse MT-3. Surprisingly, the backbone dynamics of the protein revealed that the beta-domain exhibits similar internal motion to the alpha-domain, although the N-terminal residues are more flexible. Our results may provide useful information for understanding the structure-function relationship of human MT-3.

Selected figure(s)

Figure 5.
Fig. 5. The 600 MHz two-dimensional ^1H–^15N HSQC spectrum of ^15N-labeled human Cd[7]-MT-3 in 15 mM phosphate, pH 7.3, 298 K. The assignments are indicated by residue number and one-letter amino acid code.

Figure 6.
Fig. 6. Solution structure of the α-domain of human MT-3. NMR solution structure ensembles (residues Cys34-Cys51 and Glu62-Gln68) generated by superimposing the backbone coordinates of the 10 best-converged structures (Upper). Ribbon diagram of the mean structure of α-domain of human MT-3 showing a short α-helices (Lower). Cd^2+ ions are highlighted in purple balls, and their corresponding ^113Cd resonances are labeled in Fig. 2. The atomic coordinates have been deposited in the Protein Data Bank (PDBID: 2F5H).

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2006, 580, 795-800) copyright 2006.

Figures were selected by the author.