Saccharomyces cerevisiae MT metallothionein bound to copper ions. Cysteines in yellow, copper in brown. (PDB: 1AQS)
Identifiers
Symbol
Yeast metallothionein
Pfam
PF11403
Pfam clan
CL0461
InterPro
IPR022710
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Cyanobacterial SmtA
Cyanobacterial SmtA metallothionein bound to zinc ions. Cysteines in yellow, zinc in purple. (PDB: 1JJD)
Identifiers
Symbol
Bacterial metallothionein
Pfam
PF02069
Pfam clan
CL0461
InterPro
IPR000518
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Metallothionein (MT) is a family of cysteine-rich, low molecular weight (MW ranging from 500 to 14000 Da) proteins. They are localized to the membrane of the Golgi apparatus. MTs have the capacity to bind both physiological (such as zinc, copper, selenium) and xenobiotic (such as cadmium, mercury, silver, arsenic, lead) heavy metals through the thiol group of its cysteine residues, which represent nearly 30% of its constituent amino acid residues.[2]
MT was discovered in 1957 by Vallee and Margoshe from purification of a Cd-binding protein from horse (equine) renal cortex.[3] MT plays a role in the protection against metal toxicity and oxidative stress, and is involved in zinc and copper regulation.[4] There are four main isoforms expressed in humans (family 1, see chart below): MT1 (subtypes A, B, E, F, G, H, L, M, X), MT2, MT3, and MT4. In the human body, large quantities are synthesised primarily in the liver and kidneys. Their production is dependent on availability of the dietary minerals such as zinc, copper, and selenium, as well as the amino acids histidine and cysteine.
Metallothioneins are rich in thiols, causing them to bind a number of trace metals. Metallothionein is one of the few eukaryotic proteins playing a substantial role in metal detoxification. Zinc and Cadmium are tetrahedrally coordinated to cysteine residues, and each metallothionein protein molecule may bind up to 7 atoms of Zn or Cd.[5] The biosynthesis of metallothionein appears to increase several-fold during periods of oxidative stress to shield the cells against cytotoxicity and DNA damage. Metallothionein biosynthesis can also be induced by certain hormones, pharmaceuticals, alcohols, and other compounds.[6] Metallothionein expression is upregulated during fetal development, particularly in liver tissue.[7]
^PDB: 2KAK; Peroza EA, Schmucki R, Güntert P, Freisinger E, Zerbe O (March 2009). "The beta(E)-domain of wheat E(c)-1 metallothionein: a metal-binding domain with a distinctive structure". Journal of Molecular Biology. 387 (1): 207–18. doi:10.1016/j.jmb.2009.01.035. PMID 19361445.
^Sigel H, Sigel A, eds. (2009). Metallothioneins and Related Chelators (Metal Ions in Life Sciences). Vol. 5. Cambridge, England: Royal Society of Chemistry. ISBN 978-1-84755-899-2.
^Margoshes M, Vallee BL (1957). "A cadmium protein from equine kidney cortex". Journal of the American Chemical Society. 79 (17): 4813–4814. doi:10.1021/ja01574a064.
^Felizola SJ, Nakamura Y, Arata Y, Ise K, Satoh F, Rainey WE, Midorikawa S, Suzuki S, Sasano H (September 2014). "Metallothionein-3 (MT-3) in the human adrenal cortex and its disorders". Endocrine Pathology. 25 (3): 229–35. doi:10.1007/s12022-013-9280-9. PMID 24242700. S2CID 39871076.
^Suhy DA, Simon KD, Linzer DI, O'Halloran TV (April 1999). "Metallothionein is part of a zinc-scavenging mechanism for cell survival under conditions of extreme zinc deprivation". The Journal of Biological Chemistry. 274 (14): 9183–92. doi:10.1074/jbc.274.14.9183. PMID 10092590.
^Wang WC, Mao H, Ma DD, Yang WX (August 2014). "Characteristics, functions, and applications of metallothionein in aquatic vertebrates". Frontiers in Marine Science. 1: 34. doi:10.3389/fmars.2014.00034.
^Cherian MG (September 1994). "The significance of the nuclear and cytoplasmic localization of metallothionein in human liver and tumor cells". Environmental Health Perspectives. 102 (Suppl 3): 131–5. doi:10.2307/3431776. JSTOR 3431776. PMC 1567399. PMID 7843087.
Metallothionein (MT) is a family of cysteine-rich, low molecular weight (MW ranging from 500 to 14000 Da) proteins. They are localized to the membrane...
Metallothionein-2 is a metallothionein protein that in humans is encoded by the MT2A gene. The single-nucleotide polymorphism rs28366003 which substitutes...
Metallothionein-1A is a protein that in humans is encoded by the MT1A gene. GRCh38: Ensembl release 89: ENSG00000205362 – Ensembl, May 2017 "Human PubMed...
cells. Zinc may be held in metallothionein reserves within microorganisms or in the intestines or liver of animals. Metallothionein in intestinal cells is...
Metallothionein-1G is a protein that in humans is encoded by the MT1G gene. GRCh38: Ensembl release 89: ENSG00000125144 – Ensembl, May 2017 "Human PubMed...
with metallothioneins. Thionein and metallothionein act as a redox pair, and much of the antioxidant functions of attributed to metallothionein are actually...
ISBN 978-94-007-5178-1. PMID 23430777. Freisinger EF, Vasac M (2013). "Cadmium in Metallothioneins". In Sigel A, Sigel H, Sigel RK (eds.). Cadmium: From Toxicity to Essentiality...
inflammatory cells. For example, zinc regulates the expression of metallothionein, which has multiple functions, such as intracellular zinc compartmentalization...
copper fist domain is the activation and regulation of the metallothionein gene. Metallothionein, a type of protein that binds metal in cells, is responsible...
well as other heavy metal ions like zinc or cadmium) may be bound by metallothionein and sequestered within intracellular vesicles of enterocytes (i.e....
16, 2002). "Differential expression and characterization of three metallothionein-like genes in Cavendish banana (Musa acuminata)". Physiologia Plantarum...
specific transporters and bind to storage proteins such as ferritin or metallothionein when not in use. Catabolism is the set of metabolic processes that...
Bible (Tanakh) Medial temporal, part of the temporal lobe of the brain Metallothionein, a protein Methyltransferase, a type of enzyme Microtubule, a component...
capable of concentrating zinc, a property attributed to the presence of metallothionein-like peptides in the mushroom. Russula nigricans can accumulate lead...
affinity for heavy metals, so that proteins containing cysteine, such as metallothionein, will bind metals such as mercury, lead, and cadmium tightly. In the...
is rapidly converted to insoluble silver compounds or complexed by metallothionein. However, silver fluoride and silver nitrate are caustic and can cause...
factories or workshops during pregnancy. Besides, a higher placental metallothionein (a small protein marking the exposure of toxic metals) was found among...
Aposhian, H.; Bruce, D. C. (1991). "Binding of Polonium-210 to Liver Metallothionein". Radiation Research. 126 (3): 379–382. Bibcode:1991RadR..126..379A...
Metallothionein-1F is a protein that in humans is encoded by the MT1F gene. GRCh38: Ensembl release 89: ENSG00000198417 – Ensembl, May 2017 "Human PubMed...
have shown that in Bedlingtons, the disease is caused by a defective metallothionein that causes cell lysosomes to become saturated with copper. This causes...
Metallothionein-1B is a protein that in humans is encoded by the MT1B gene. GRCh38: Ensembl release 89: ENSG00000169688 – Ensembl, May 2017 "Human PubMed...
Metallothionein-1H is a protein that in humans is encoded by the MT1H gene. GRCh38: Ensembl release 89: ENSG00000205358 – Ensembl, May 2017 "Human PubMed...
rise, 13,500–14,700 years ago Melatonin receptor 1A, a human gene Metallothionein 1A, a human gene MH-1A, a nuclear power reactor and the first floating...
Metallothionein-1E is a protein that in humans is encoded by the MT1E gene. GRCh38: Ensembl release 89: ENSG00000169715 – Ensembl, May 2017 "Human PubMed...
Global Information
