2VKC

Solution structure of the B3BP Smr domain

2VKC の概要

• エントリーDOI: 10.2210/pdb2vkc/pdb
• 関連するPDBエントリー: 2D9I
• 分子名称: NEDD4-BINDING PROTEIN 2 (1 entity in total)
• 機能のキーワード: human bcl3 binding protein, alternative splicing, homologous recombination, mismatch repair, small muts related, nucleotide-binding, atp-binding, ubl conjugation, phosphorylation, smr, b3bp, hydrolase, cytoplasm, coiled coil
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm (By similarity): Q86UW6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15189.63

構造登録者

Diercks, T.,Ab, E.,Daniels, M.A.,deJong, R.N.,Besseling, R.,Kaptein, R.,Folkers, G.E. (登録日: 2007-12-18, 公開日: 2008-10-14, 最終更新日: 2024-05-15)

主引用文献

Diercks, T.,Ab, E.,Daniels, M.A.,De Jong, R.N.,Besseling, R.,Kaptein, R.,Folkers, G.E.
Solution Structure and Characterization of the DNA- Binding Activity of the B3BP-Smr Domain.
J.Mol.Biol., 383:1156-, 2008

PubMed Abstract: The MutS1 protein recognizes unpaired bases and initiates mismatch repair, which are essential for high-fidelity DNA replication. The homologous MutS2 protein does not contribute to mismatch repair, but suppresses homologous recombination. MutS2 lacks the damage-recognition domain of MutS1, but contains an additional C-terminal extension: the small MutS-related (Smr) domain. This domain, which is present in both prokaryotes and eukaryotes, has previously been reported to bind to DNA and to possess nicking endonuclease activity. We determine here the solution structure of the functionally active Smr domain of the Bcl3-binding protein (also known as Nedd4-binding protein 2), a protein with unknown function that lacks other domains present in MutS proteins. The Smr domain adopts a two-layer alpha-beta sandwich fold, which has a structural similarity to the C-terminal domain of IF3, the R3H domain, and the N-terminal domain of DNase I. The most conserved residues are located in three loops that form a contiguous, exposed, and positively charged surface with distinct sequence identity for prokaryotic and eukaryotic Smr domains. NMR titration experiments and DNA binding studies using Bcl3-binding protein-Smr domain mutants suggested that these most conserved loop regions participate in DNA binding to single-stranded/double-stranded DNA junctions. Based on the observed DNA-binding-induced multimerization, the structural similarity with both subdomains of DNase I, and the experimentally identified DNA-binding surface, we propose a model for DNA recognition by the Smr domain.

PubMed: 18804481
DOI: 10.1016/J.JMB.2008.09.005

実験手法

SOLUTION NMR