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PDBsum entry 6b8f

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protein metals links
Oxidoreductase PDB id
6b8f

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
172 a.a.
Metals
_CA ×11
_FE ×2
Waters ×340
PDB id:
6b8f
Name: Oxidoreductase
Title: Contracted human heavy-chain ferritin crystal-hydrogel hybrid
Structure: Ferritin heavy chain. Chain: a. Synonym: ferritin h subunit,cell proliferation-inducing gene 15 protein. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: fth1, fth, fthl6, ok/sw-cl.84, pig15. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.06Å     R-factor:   0.092     R-free:   0.103
Authors: L.Zhang,J.B.Bailey,R.Subramanian,F.A.Tezcan
Key ref: L.Zhang et al. (2018). Hyperexpandable, self-healing macromolecular crystals with integrated polymer networks. Nature, 557, 86-91. PubMed id: 29720635 DOI: 10.1038/s41586-018-0057-7
Date:
07-Oct-17     Release date:   02-May-18    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P02794  (FRIH_HUMAN) -  Ferritin heavy chain from Homo sapiens
Seq:
Struc:
183 a.a.
172 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.1.16.3.1  - ferroxidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 4 Fe2+ + O2 + 4 H+ = 4 Fe3+ + 2 H2O
4 × Fe(2+)
+ O2
+ 4 × H(+)
= 4 × Fe(3+)
+ 2 × H2O
      Cofactor: Cu cation
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Key reference    
 
 
DOI no: 10.1038/s41586-018-0057-7 Nature 557:86-91 (2018)
PubMed id: 29720635  
 
 
Hyperexpandable, self-healing macromolecular crystals with integrated polymer networks.
L.Zhang, J.B.Bailey, R.H.Subramanian, F.A.Tezcan.
 
  ABSTRACT  
 
The formation of condensed matter typically involves a trade-off between structural order and flexibility. As the extent and directionality of interactions between atomic or molecular components increase, materials generally become more ordered but less compliant, and vice versa. Nevertheless, high levels of structural order and flexibility are not necessarily mutually exclusive; there are many biological (such as microtubules1,2, flagella 3 , viruses4,5) and synthetic assemblies (for example, dynamic molecular crystals6-9 and frameworks10-13) that can undergo considerable structural transformations without losing their crystalline order and that have remarkable mechanical properties8,14,15 that are useful in diverse applications, such as selective sorption 16 , separation 17 , sensing 18 and mechanoactuation 19 . However, the extent of structural changes and the elasticity of such flexible crystals are constrained by the necessity to maintain a continuous network of bonding interactions between the constituents of the lattice. Consequently, even the most dynamic porous materials tend to be brittle and isolated as microcrystalline powders 14 , whereas flexible organic or inorganic molecular crystals cannot expand without fracturing. Owing to their rigidity, crystalline materials rarely display self-healing behaviour 20 . Here we report that macromolecular ferritin crystals with integrated hydrogel polymers can isotropically expand to 180 per cent of their original dimensions and more than 500 per cent of their original volume while retaining periodic order and faceted Wulff morphologies. Even after the separation of neighbouring ferritin molecules by 50 ångströms upon lattice expansion, specific molecular contacts between them can be reformed upon lattice contraction, resulting in the recovery of atomic-level periodicity and the highest-resolution ferritin structure reported so far. Dynamic bonding interactions between the hydrogel network and the ferritin molecules endow the crystals with the ability to resist fragmentation and self-heal efficiently, whereas the chemical tailorability of the ferritin molecules enables the creation of chemically and mechanically differentiated domains within single crystals.
 

 

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