Engineering the metal-binding loop at a type 1 copper center by circular permutation
Author:
Affiliation:
1. College of Biotechnology
2. Tianjin University of Science and Technology
3. Tianjin
4. China
5. Tianjin Institute of Industrial Biotechnology
6. Chinese Academy of Sciences
7. Laboratory of RNA Biology
8. Institute of Biophysics
9. Beijing
Abstract
Circular permutation of the cupredoxin azurin creates a break on the metal binding loop, highlighting the loop's flexibility.
Funder
National Natural Science Foundation of China
Youth Innovation Promotion Association of the Chinese Academy of Sciences
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2017/RA/C7RA11512A
Reference46 articles.
1. Engineering type 1 copper sites in proteins
2. Copper coordination in blue proteins
3. Nuclear magnetic resonance spectroscopy studies on copper proteins
4. Investigating the structure and function of cupredoxins
5. Design of functional metalloproteins
Cited by 4 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Protein engineering using circular permutation – structure, function, stability, and applications;The FEBS Journal;2024-04-27
2. Circular permutation at azurin’s active site slows down its folding;JBIC Journal of Biological Inorganic Chemistry;2023-11-13
3. Metal‐binding and circular permutation‐dependent thermodynamic and kinetic stability of azurin;Proteins: Structure, Function, and Bioinformatics;2022-12-27
4. An engineered azurin with a lanthanide binding site capable of copper sensing;Biochemical and Biophysical Research Communications;2021-07
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