3HF1

Crystal structure of human p53R2

3HF1 の概要

• エントリーDOI: 10.2210/pdb3hf1/pdb
• 関連するPDBエントリー: 1W68 1W69 1XSM 2UW2
• 分子名称: Ribonucleoside-diphosphate reductase subunit M2 B, FE (III) ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: p53 inducible, ribonucleotide reductase small subunit, disease mutation, dna damage, dna repair, dna replication, iron, metal-binding, nucleus, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q7LG56
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81922.39

構造登録者

Smith, P.,Zhou, B.,Yuan, Y.-C.,Su, L.,Tsai, S.-C.,Yen, Y. (登録日: 2009-05-10, 公開日: 2009-10-13, 最終更新日: 2023-09-06)

主引用文献

Smith, P.,Zhou, B.,Ho, N.,Yuan, Y.C.,Su, L.,Tsai, S.C.,Yen, Y.
2.6 A X-ray crystal structure of human p53R2, a p53-inducible ribonucleotide reductase .
Biochemistry, 48:11134-11141, 2009

PubMed Abstract: Human p53R2 (hp53R2) is a 351-residue p53-inducible ribonucleotide reductase (RNR) small subunit. It shares >80% sequence identity with hRRM2, the small RNR subunit responsible for normal maintenance of the deoxyribonucleotide (dNTP) pool used for DNA replication, which is active during the S phase in a cell cycle-dependent fashion. But rather than cyclic dNTP synthesis, hp53R2 has been shown to supply dNTPs for DNA repair to cells in G0-G1 in a p53-dependent fashion. The first X-ray crystal structure of hp53R2 is determined to 2.6 A, in which monomers A and B exhibit mono- and binuclear iron occupancy, respectively. The pronounced structural differences at three regions between hp53R2 and hRRM2 highlight the possible regulatory role in iron assimilation and help explain previously observed physical and biochemical differences in the mobility and accessibility of the radical iron center, as well as radical transfer pathways between the two enzymes. The sequence-structure-function correlations that differentiate hp53R2 and hRRM2 are revealed for the first time. Insight gained from this structural work will be used in the identification of biological function, regulation mechanism, and inhibitor selection in RNR small subunits.

PubMed: 19728742
DOI: 10.1021/bi9001425

実験手法

X-RAY DIFFRACTION (2.6 Å)