PDBsum entry 7jgo

Oxidoreductase

PDB id: 7jgo

Contents

Protein chain

173 a.a.

Ligands

V9Y

Metals

_NA

_NI ×3

Waters ×25

PDB id:

7jgo

Name:

Oxidoreductase

Title:

Crystal structure of the ni-bound human heavy-chain variant 122h-delta c-star with 2,5-furandihyrdoxamate collected at 278k

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:

3.08Å R-factor: 0.213 R-free: 0.248

Authors:

J.B.Bailey,F.A.Tezcan

Key ref:

J.B.Bailey and F.A.Tezcan (2020). Tunable and Cooperative Thermomechanical Properties of Protein-Metal-Organic Frameworks. J Am Chem Soc, 142, 17265-17270. PubMed id: 32972136 DOI: 10.1021/jacs.0c07835

Date:

19-Jul-20 Release date: 14-Oct-20

Protein chain

P02794  (FRIH_HUMAN) -  Ferritin heavy chain from Homo sapiens

Seq: 183 a.a.

Struc: 173 a.a.*

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.1.16.3.1 - ferroxidase.
• Reaction: 4 Fe²⁺ + O2 + 4 H⁺ = 4 Fe³⁺ + 2 H2O
• Cofactor: Cu cation

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Key reference

DOI no: 10.1021/jacs.0c07835

J Am Chem Soc 142:17265-17270 (2020)

PubMed id: 32972136

Tunable and Cooperative Thermomechanical Properties of Protein-Metal-Organic Frameworks.

J.B.Bailey, F.A.Tezcan.

ABSTRACT

We recently introduced protein-metal-organic frameworks (protein-MOFs) as chemically designed protein crystals, composed of ferritin nodes that predictably assemble into 3D lattices upon coordination of various metal ions and ditopic, hydroxamate-based linkers. Owing to their unique tripartite construction, protein-MOFs possess extremely sparse lattice connectivity, suggesting that they might display unusual thermomechanical properties. Leveraging the synthetic modularity of ferritin-MOFs, we investigated the temperature-dependent structural dynamics of six distinct frameworks. Our results show that the thermostabilities of ferritin-MOFs can be tuned through the metal component or the presence of crowding agents. Our studies also reveal a framework that undergoes a reversible and isotropic first-order phase transition near-room temperature, corresponding to a 4% volumetric change within 1 °C and a hysteresis window of ∼10 °C. This highly cooperative crystal-to-crystal transformation, which stems from the soft crystallinity of ferritin-MOFs, illustrates the advantage of modular construction strategies in discovering tunable-and unpredictable-material properties.