1BNO

NMR SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF DNA POLYMERASE BETA, MINIMIZED AVERAGE STRUCTURE

1BNO の概要

• エントリーDOI: 10.2210/pdb1bno/pdb
• 分子名称: DNA POLYMERASE BETA (1 entity in total)
• 機能のキーワード: n-terminal domain, dna polymerase beta, single-stranded dna-binding, nucleotidyltransferase, nucleotidyltransferase (dna-binding)
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Nucleus: P06766
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9632.30

構造登録者

Liu, D.-J.,Prasad, R.,Wilson, S.H.,Derose, E.F.,Mullen, G.P. (登録日: 1996-04-25, 公開日: 1996-12-07, 最終更新日: 2024-05-22)

主引用文献

Liu, D.,Prasad, R.,Wilson, S.H.,DeRose, E.F.,Mullen, G.P.
Three-dimensional solution structure of the N-terminal domain of DNA polymerase beta and mapping of the ssDNA interaction interface.
Biochemistry, 35:6188-6200, 1996

PubMed Abstract: DNA polymerase beta (beta-Pol) consists of an N-terminal ssDNA binding domain with deoxyribose phosphodiesterase activity and a C-terminal domain with nucleotidyltransferase activity. The solution structure of the cloned N-terminal domain of beta-Pol has been determined by multidimensional heteronuclear NMR using experimental restraints that included 1030 distances based on analysis of NOE connectivities, 68 phi, chi 1, and chi 2 torsion angles based on analysis of couplings, and 22 hydrogen bonds. Hydrogen bonds were assessed only within helices by the absence of saturation transfer from water at pH 6.7, by NOEs and JNH alpha couplings indicative of well-structured helices, and by 13C alpha chemical shifts characteristic of helices. The root mean square deviation for heavy backbone atoms within the helices was 0.64 A in 55 structures. The solution structure of the N-terminal domain is formed from four helices packed as two antiparallel pairs crossing at 50 degrees in a V-like shape. The domain binds p(dT)8, a template analogue, as a 1:1 complex in 100 mM NaCl (KD = 10 microM). Analysis of the binding equilibria at increasing NaCl concentrations indicated that ionic contacts contribute to the complex. The binding interaction was mapped to one face of the domain by characterizing backbone 1H and 15N chemical shift changes. Assigned intermolecular NOEs from 2D NOESY support the assessment of the binding interface. The structure that forms the interaction surface includes an antiparallel helix-3-turn-helix-4 motif and residues adjacent to an omega-type loop connecting helix-1 and helix-2. Sites appropriate for nucleotide contact on the structure are described. The mapped interaction interface for a ssDNA template is the first described for a DNA polymerase.

PubMed: 8639559
DOI: 10.1021/bi952656o

実験手法

SOLUTION NMR