1IUF

LOW RESOLUTION SOLUTION STRUCTURE OF THE TWO DNA-BINDING DOMAINS IN Schizosaccharomyces pombe ABP1 PROTEIN

1IUF の概要

• エントリーDOI: 10.2210/pdb1iuf/pdb
• 分子名称: centromere abp1 protein (1 entity in total)
• 機能のキーワード: centromere, riken structural genomics/proteomics initiative, rsgi, structural genomics, dna binding protein
• 由来する生物種: Schizosaccharomyces pombe (fission yeast)
• 細胞内の位置: Nucleus: P49777
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17086.40

構造登録者

Kikuchi, J.,Iwahara, J.,Kigawa, T.,Murakami, Y.,Okazaki, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2002-03-04, 公開日: 2002-06-05, 最終更新日: 2023-12-27)

主引用文献

Kikuchi, J.,Iwahara, J.,Kigawa, T.,Murakami, Y.,Okazaki, T.,Yokoyama, S.
Solution structure determination of the two DNA-binding domains in the Schizosaccharomyces pombe Abp1 protein by a combination of dipolar coupling and diffusion anisotropy restraints.
J.Biomol.NMR, 22:333-347, 2002

PubMed Abstract: We have solved the solution structure of the N-terminal region of the fission yeast centromere protein, Abp1, bound to a 21-base pair DNA fragment bearing its recognition site (Mw = 30 kDa). Although the two DNA-binding domains in the Abpl protein were defined well by a conventional NOE-based NMR methodology, the overall structure of the Abpl protein was poorly defined, due to the lack of interdomain distance restraints. Therefore, we additionally used residual dipolar couplings measured in a weakly aligned state, and rotational diffusion anisotropies. Neither the NH residual dipolar couplings nor the backbone 15N T1/T2 data were sufficient to determine the overall structure of the Abpl protein, due to spectral overlap. We used a combination of these two orientational restraints (residual dipolar coupling and rotational diffusion anisotropy), which significantly improved the convergence of the overall structures. The range of the observed T1/T2 ratios was wider (20-50 for the secondary structure regions of Abp 1) than the previously reported data for several globular proteins, indicating that the overall shape of the Abp1.DNA complex is ellipsoid. This extended form would facilitate the recognition of the two separate sites in the relatively long DNA sequence by the DNA-binding domains of Apb1.

PubMed: 12018481
DOI: 10.1023/A:1014977808170

実験手法

SOLUTION NMR