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Related Concept Videos

Metal-Ligand Bonds02:51

Metal-Ligand Bonds

The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
Protein Transport to the Inner Chloroplast Membrane01:18

Protein Transport to the Inner Chloroplast Membrane

Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
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Complexation Equilibria: Factors Influencing Stability of Complexes01:09

Complexation Equilibria: Factors Influencing Stability of Complexes

In complexation reactions, metal cations are the electron pair acceptors, and the ligands are the electron pair donors. The stability of the metal complexes depends primarily on the complexing ability of the central metal ion and the nature of the ligands. Generally, the complexing ability of the metal ion depends on the size and charge of the ion. As the metal ion size increases, the stability of the metal complexes decreases, provided that the valency of the metal ion and the ligands remain...

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Updated: May 31, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Structural features specific to plant metallothioneins.

Eva Freisinger1

  • 1Institute of Inorganic Chemistry, University of Zurich, 8057, Zurich, Switzerland. freisinger@aci.uzh.ch

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|June 21, 2011
PubMed
Summary

Plant metallothioneins (MTs) exhibit unique structural features due to sequence diversity and long linkers. This review explores known and deduced structural aspects of plant MTs, focusing on metal-binding and cluster arrangements.

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Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
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Last Updated: May 31, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Published on: December 16, 2013

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis
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Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

Area of Science:

  • Biochemistry
  • Structural Biology
  • Plant Science

Background:

  • Metallothioneins (MTs) are cysteine-rich proteins coordinating metal ions across diverse life forms.
  • Plant MTs show significant sequence diversity, necessitating further classification into subfamilies.
  • Long, cysteine-free linker regions in plant MTs present unique structural and functional questions.

Purpose of the Study:

  • To review and synthesize current knowledge on the structural features of plant metallothioneins.
  • To highlight the importance of understanding plant MT structure for metal ion coordination.
  • To identify knowledge gaps and areas for future research in plant MT structural biology.

Main Methods:

  • Analysis of existing structural data, including the 3D structure of wheat E(c)-1 MT.
  • Spectroscopic techniques such as circular dichroism, IR, and Raman spectroscopy to determine secondary structures.
  • Limited proteolytic digestion to assess the spatial arrangement of cysteine-rich regions.
  • Evaluation of metal ion content and metal-thiolate cluster structures.

Main Results:

  • The plant MT family displays considerable sequence diversity, leading to distinct structural characteristics.
  • The wheat E(c)-1 MT structure revealed unprecedented metal cluster arrangements.
  • Spectroscopic and proteolytic digestion methods provide insights into secondary structures and linker region influences.
  • Metal ion to cysteine ratios are critical for predicting metal-thiolate cluster formation.

Conclusions:

  • Plant MTs possess unique structural attributes, including long linkers and novel metal-binding configurations.
  • Further structural elucidation of plant MTs is crucial for understanding their diverse functions.
  • Integrating spectroscopic, biochemical, and structural data is essential for a comprehensive understanding of plant MTs.