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PDBsum entry 1dft
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protein metals links
Metal binding protein PDB id
1dft

 

 

 

 

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Contents
Protein chain
30 a.a.
Metals
_CD ×3
PDB id:
1dft
Name: Metal binding protein
Title: Solution structure of the beta-domain of mouse metallothionein-1
Structure: Metallothionein-1. Chain: a. Fragment: n-terminal domain (beta). Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 1 models
Authors: K.Zangger,G.Oz,J.D.Otvos,I.M.Armitage
Key ref: K.Zangger et al. (1999). Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy. Protein Sci, 8, 2630-2638. PubMed id: 10631978 DOI: 10.1110/ps.8.12.2630
Date:
20-Nov-99     Release date:   01-Dec-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P02802  (MT1_MOUSE) -  Metallothionein-1 from Mus musculus
Seq:
Struc: 		61 a.a.
30 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1110/ps.8.12.2630 Protein Sci 8:2630-2638 (1999)
PubMed id: 10631978  
 
 
Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy.
K.Zangger, G.Oz, J.D.Otvos, I.M.Armitage.
 
  ABSTRACT  
 
Sequential 1H-NMR assignments of mouse [Cd7]-metallothionein-1 (MT1) have been carried out by standard homonuclear NMR methods and the use of an accordion-heteronuclear multiple quantum correlation (HMQC) experiment for establishing the metal, 113Cd2+, to cysteine connectivities. The three-dimensional structure was then calculated using the distance constraints from two-dimensional nuclear Overhauser effect (NOE) spectroscopy spectra and the Cys-Cd connectivities as input for a distance geometry-dynamical simulated annealing protocol in X-PLOR 3.851. Similar to the mammalian MT2 isoforms, the homologous primary structure of MT1 suggested two separate domains, each containing one metal cluster. Because there were no interdomain constraints, the structure calculation for the N-terminal beta- and the C-terminal alpha-domain were carried out separately. The structures are based on 409 NMR constraints, consisting of 381 NOEs and 28 cysteine-metal connectivities. The only elements of regular secondary structure found were two short stretches of 3(10) helices along with some half-turns in the alpha-domain. Structural comparison with rat liver MT2 showed high similarity, with the beta-domain structure in mouse MT1 showing evidence of increased flexibility compared to the same domain in MT2. The latter was reflected by the presence of fewer interresidue NOEs, no slowly exchanging backbone amide protons, and enhanced cadmium-cadmium exchange rates found in the beta-domain of MT1.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20442962 C.A.Blindauer, and O.I.Leszczyszyn (2010).
Metallothioneins: unparalleled diversity in structures and functions for metal ion homeostasis and more.
  Nat Prod Rep, 27, 720-741.  
  21234102 I.El Ghazi, B.L.Martin, and I.M.Armitage (2010).
New proteins found interacting with brain metallothionein-3 are linked to secretion.
  Int J Alzheimers Dis, 2011, 208634.  
19609577 N.Romero-Isart, B.Oliva, and M.Vasák (2010).
Influence of NH-Sgamma bonding interactions on the structure and dynamics of metallothioneins.
  J Mol Model, 16, 387-394.  
18157556 H.Wang, H.Li, B.Cai, Z.X.Huang, and H.Sun (2008).
The effect of nitric oxide on metal release from metallothionein-3: gradual unfolding of the protein.
  J Biol Inorg Chem, 13, 411-419.  
17403038 B.Dolderer, H.Echner, A.Beck, H.J.Hartmann, U.Weser, C.Luchinat, and C.Del Bianco (2007).
Coordination of three and four Cu(I) to the alpha- and beta-domain of vertebrate Zn-metallothionein-1, respectively, induces significant structural changes.
  FEBS J, 274, 2349-2362.  
17211631 E.A.Peroza, and E.Freisinger (2007).
Metal ion binding properties of Triticum [corrected] aestivum Ec-1 metallothionein: evidence supporting two separate metal thiolate clusters.
  J Biol Inorg Chem, 12, 377-391.  
17427961 F.Y.Ni, B.Cai, Z.C.Ding, F.Zheng, M.J.Zhang, H.M.Wu, H.Z.Sun, and Z.X.Huang (2007).
Structural prediction of the beta-domain of metallothionein-3 by molecular dynamics simulation.
  Proteins, 68, 255-266.  
16240177 A.M.Zimeri, O.P.Dhankher, B.McCaig, and R.B.Meagher (2005).
The plant MT1 metallothioneins are stabilized by binding cadmiums and are required for cadmium tolerance and accumulation.
  Plant Mol Biol, 58, 839-855.  
15182356 L.Khatai, W.Goessler, H.Lorencova, and K.Zangger (2004).
Modulation of nitric oxide-mediated metal release from metallothionein by the redox state of glutathione in vitro.
  Eur J Biochem, 271, 2408-2416.  
15511227 P.A.Cobine, R.T.McKay, K.Zangger, C.T.Dameron, and I.M.Armitage (2004).
Solution structure of Cu6 metallothionein from the fungus Neurospora crassa.
  Eur J Biochem, 271, 4213-4221.
PDB code: 1t2y
11835501 C.Capasso, O.Abugo, F.Tanfani, A.Scire, V.Carginale, R.Scudiero, E.Parisi, and S.D'Auria (2002).
Stability and conformational dynamics of metallothioneins from the antarctic fish Notothenia coriiceps and mouse.
  Proteins, 46, 259-267.  
11284699 L.S.Busenlehner, N.J.Cosper, R.A.Scott, B.P.Rosen, M.D.Wong, and D.P.Giedroc (2001).
Spectroscopic properties of the metalloregulatory Cd(II) and Pb(II) sites of S. aureus pI258 CadC.
  Biochemistry, 40, 4426-4436.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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