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8OZS

Populus tremula stable protein 1 with N-terminal binding peptide extension with hemin

Summary for 8OZS
Entry DOI10.2210/pdb8ozs/pdb
DescriptorStable protein 1 (2 entities in total)
Functional Keywordshemine, protein engineering, biohybrid, catalysis, plant protein
Biological sourcePopulus tremula
Total number of polymer chains24
Total formula weight328352.78
Authors
Sklyar, J.,Zeibaq, Y.,Bachar, O.,Yehezkeli, O.,Adir, N. (deposition date: 2023-05-09, release date: 2024-03-27, Last modification date: 2025-04-23)
Primary citationZeibaq, Y.,Bachar, O.,Sklyar, J.,Adir, N.,Yehezkeli, O.
A Bioengineered Stable Protein 1-Hemin Complex with Enhanced Peroxidase-Like Catalytic Properties.
Small Sci, 4:2400025-2400025, 2024
Cited by
PubMed Abstract: Enzymes have gained their unique efficiency and catalytic activity through billions of years of evolution, perfecting their active site to a desired reaction. Inspired by nature, a novel enzyme-mimicking platform is designed based on stable protein 1 (SP1) to create a nano-compartment that mimics peroxidase activity. The biohybrid reveals enhanced activity over the hemin cofactor alone and improved stability in organic solvents in comparison to native peroxidase. Furthermore, the utilization of the obtained biohybrid in an optical glucose biosensing platform is shown. The biohybrid crystallographic structure is solved, indicating that the SP1 structure is not affected by the hemin coordination. This work opens the path for developing new cofactor binding centers in engineered protein scaffolds for various artificial catalytic processes.
PubMed: 40212758
DOI: 10.1002/smsc.202400025
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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数据于2025-10-29公开中

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