TUHH Open Research
Help
  • Log In
    New user? Click here to register.Have you forgotten your password?
  • English
  • Deutsch
  • Communities & Collections
  • Publications
  • Research Data
  • People
  • Institutions
  • Projects
  • Statistics
  1. Home
  2. TUHH
  3. Publications
  4. Structure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step
 
Options

Structure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step

Citation Link: https://doi.org/10.15480/882.3518
Publikationstyp
Journal Article
Date Issued
2020-12
Sprache
English
Author(s)
Zhang, Han  
Li, Yuchen  
Nie, Jinglei  
Ren, Jie  
Zeng, An-Ping  orcid-logo
Institut
Bioprozess- und Biosystemtechnik V-1  
TORE-DOI
10.15480/882.3518
TORE-URI
http://hdl.handle.net/11420/8445
Journal
Communications biology  
Volume
3
Issue
1
Article Number
756
Citation
Communications Biology 3 (1): 756 (2020-12)
Publisher DOI
10.1038/s42003-020-01401-6
Scopus ID
2-s2.0-85097493734
PubMed ID
33311647
Publisher
Springer Nature
Molecular shuttles play decisive roles in many multi-enzyme systems such as the glycine cleavage system (GCS) for one-carbon (C1) metabolism. In GCS, a lipoate swinging arm containing an aminomethyl moiety is attached to protein H and serves as a molecular shuttle among different proteins. Protection of the aminomethyl moiety in a cavity of protein H and its release induced by protein T are key processes but barely understood. Here, we present a detailed structure-based dynamic analysis of the induced release of the lipoate arm of protein H. Based on molecular dynamics simulations of interactions between proteins H and T, four major steps of the release process showing significantly different energy barriers and time scales can be distinguished. Mutations of a key residue, Ser-67 in protein H, led to a bidirectional tuning of the release process. This work opens ways to target C1 metabolism in biomedicine and the utilization of formate and CO2 for biosynthesis.
DDC Class
600: Technik
Funding(s)
Publikationsfonds 2020  
Neue Ansätze zur populationsbasierten kinetischen Untersuchung und Modellierung von Hochzelldichte-Zellkulturen  
Funding Organisations
Deutsche Forschungsgemeinschaft (DFG)  
More Funding Information
This work was financially supported by the Beijing Advanced Innovation Center for Soft Matter Science and Engineering and by the Deutsche Forschungsgemeinschaft (DFG) through the project ZE 542/12-1 within the priority program SPP 1934.
Publication version
publishedVersion
Lizenz
https://creativecommons.org/licenses/by/4.0/
No Thumbnail Available
Name

s42003-020-01401-6.pdf

Size

3.98 MB

Format

Adobe PDF

Scopus© citations
12
Acquisition Date
Jun 30, 2024
View Details
Altmetric badge is blocked by your
consent settings
Dimensions badge is blocked by your
consent settings
Views
154
Acquisition Date
Jul 4, 2025
View Details
Downloads
156
Last Month
2
Acquisition Date
Jul 4, 2025
View Details
Google Scholar
TUHH
Weiterführende Links
  • Contact
  • Send Feedback
  • Cookie settings
  • Privacy policy
  • Impress
DSpace Software

Built with DSpace-CRIS software - Extension maintained and optimized by 4Science
Design by effective webwork GmbH

  • Deutsche NationalbibliothekDeutsche Nationalbibliothek
  • ORCiD Member OrganizationORCiD Member Organization
  • DataCiteDataCite
  • Re3DataRe3Data
  • OpenDOAROpenDOAR
  • OpenAireOpenAire
  • BASE Bielefeld Academic Search EngineBASE Bielefeld Academic Search Engine
Feedback

We collect and process your personal information for the following purposes: Authentication, Preferences, Acknowledgement and Statistics.
To learn more, please read our
privacy policy.

Customize