Conformational changes of DNA repair glycosylase MutM triggered by DNA binding
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F20%3A00531389" target="_blank" >RIV/61388963:_____/20:00531389 - isvavai.cz</a>
Result on the web
<a href="https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.13876" target="_blank" >https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.13876</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/1873-3468.13876" target="_blank" >10.1002/1873-3468.13876</a>
Alternative languages
Result language
angličtina
Original language name
Conformational changes of DNA repair glycosylase MutM triggered by DNA binding
Original language description
Bacterial MutM is a DNA repair glycosylase removing DNA damage generated from oxidative stress and, therefore, preventing mutations and genomic instability. MutM belongs to the Fpg/Nei family of prokaryotic enzymes sharing structural and functional similarities with their eukaryotic counterparts, for example, NEIL1–NEIL3. Here, we present two crystal structures of MutM from pathogenic Neisseria meningitidis : a MutM holoenzyme and MutM bound to DNA. The free enzyme exists in an open conformation, while upon binding to DNA, both the enzyme and DNA undergo substantial structural changes and domain rearrangement. Our data show that not only NEI glycosylases but also the MutMs undergo dramatic conformational changes. Moreover, crystallographic data support the previously published observations that MutM enzymes are rather flexible and dynamic molecules.
Czech name
—
Czech description
—
Classification
Type
J<sub>SC</sub> - Article in a specialist periodical, which is included in the SCOPUS database
CEP classification
—
OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/GJ17-21649Y" target="_blank" >GJ17-21649Y: Dissecting the mechanisms and the role of FANCD2 monoubiquitylation in DNA crosslink repair</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
FEBS Letters
ISSN
0014-5793
e-ISSN
—
Volume of the periodical
594
Issue of the periodical within the volume
18
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
13
Pages from-to
3032-3044
UT code for WoS article
000551286700001
EID of the result in the Scopus database
2-s2.0-85088400873