2KMG

The structure of the KlcA and ArdB proteins show a novel fold and antirestriction activity against Type I DNA restriction systems in vivo but not in vitro

2KMG の概要

• エントリーDOI: 10.2210/pdb2kmg/pdb
• NMR情報: BMRB: 16428
• 分子名称: KlcA (1 entity in total)
• 機能のキーワード: klca, ardb, nmr spectroscopy, anti-restriction, plasmid, gene regulation
• 由来する生物種: Bordetella pertussis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15673.63

構造登録者

Serfiotis-Mitsa, D.,Herbert, A.P.,Roberts, G.A.,Soares, D.C.,White, J.H.,Blakely, G.W.,Uhrin, D.,Dryden, D.T.F. (登録日: 2009-07-28, 公開日: 2009-12-29, 最終更新日: 2024-05-15)

主引用文献

Serfiotis-Mitsa, D.,Herbert, A.P.,Roberts, G.A.,Soares, D.C.,White, J.H.,Blakely, G.W.,Uhrin, D.,Dryden, D.T.F.
The structure of the KlcA and ArdB proteins reveals a novel fold and antirestriction activity against Type I DNA restriction systems in vivo but not in vitro
Nucleic Acids Res., 38:1723-1737, 2010

PubMed Abstract: Plasmids, conjugative transposons and phage frequently encode anti-restriction proteins to enhance their chances of entering a new bacterial host that is highly likely to contain a Type I DNA restriction and modification (RM) system. The RM system usually destroys the invading DNA. Some of the anti-restriction proteins are DNA mimics and bind to the RM enzyme to prevent it binding to DNA. In this article, we characterize ArdB anti-restriction proteins and their close homologues, the KlcA proteins from a range of mobile genetic elements; including an ArdB encoded on a pathogenicity island from uropathogenic Escherichia coli and a KlcA from an IncP-1b plasmid, pBP136 isolated from Bordetella pertussis. We show that all the ArdB and KlcA act as anti-restriction proteins and inhibit the four main families of Type I RM systems in vivo, but fail to block the restriction endonuclease activity of the archetypal Type I RM enzyme, EcoKI, in vitro indicating that the action of ArdB is indirect and very different from that of the DNA mimics. We also present the structure determined by NMR spectroscopy of the pBP136 KlcA protein. The structure shows a novel protein fold and it is clearly not a DNA structural mimic.

PubMed: 20007596
DOI: 10.1093/nar/gkp1144

実験手法

SOLUTION NMR