Home LiteratureArticle Details
PMID: 7773746 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

DNA modification by methyltransferases.

Current opinion in structural biology ·Vol. 5 ·No. 1 ·1995-02-00 ·Pages 4-10

Cheng X

Abstract

Enzymatic methylation of DNA plays important roles in both prokaryotes and eukaryotes. Structural study of the HhaI DNA methyltransferase has provided considerable insight into the chemistry of C5-cytosine methylation. The DNA-protein complex reveals a substrate cytosine flipped out of the double helix during the reaction, and a novel two-loop DNA-binding motif used for both sequence recognition and flipping the base. Structural comparison of HhaI C5-cytosine methyltransferase, TaqI N6-adenine methyltransferase, and catechol O-methyltransferase reveals a common catalytic domain structure, which might be universal among S-adenosyl-L-methionine (SAM)-dependent methyltransferases.

MeSH Terms
Amino Acid Sequence Animals DNA/chemistry,metabolism Humans Methyltransferases/chemistry,pharmacology Molecular Sequence Data Nucleic Acid Conformation/drug effects
Chemicals
DNA Methyltransferases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Cheng X
WM Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, New York 11724, USA.
Article Info
Journal
Current opinion in structural biology
Abbr.
Curr Opin Struct Biol
ISSN
0959-440X
Published
1995-02-00
Pages
4-10
Language
English
Region
England
NLM ID
9107784
Subset
IM
Grants
NIGMS NIH HHS · GM 49245 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]