1L1L

CRYSTAL STRUCTURE OF B-12 DEPENDENT (CLASS II) RIBONUCLEOTIDE REDUCTASE

1L1L の概要

• エントリーDOI: 10.2210/pdb1l1l/pdb
• 分子名称: RIBONUCLEOSIDE TRIPHOSPHATE REDUCTASE (2 entities in total)
• 機能のキーワード: 10-stranded alpha-beta barrel, central finger loop, oxidoreductase
• 由来する生物種: Lactobacillus leichmannii
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 328283.88

構造登録者

Sintchak, M.D.,Arjara, G.,Kellogg, B.A.,Stubbe, J.,Drennan, C.L. (登録日: 2002-02-18, 公開日: 2002-04-10, 最終更新日: 2024-10-16)

主引用文献

Sintchak, M.D.,Arjara, G.,Kellogg, B.A.,Stubbe, J.,Drennan, C.L.
The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer.
Nat.Struct.Biol., 9:293-300, 2002

PubMed Abstract: Ribonucleotide reductases (RNRs) catalyze the conversion of ribonucleotides to deoxyribonucleotides, an essential step in DNA biosynthesis and repair. Here we present the crystal structure of class II (coenzyme B12-dependent) ribonucleoside triphosphate reductase (RTPR) from Lactobacillus leichmannii in the apo enzyme form and in complex with the B12 analog adeninylpentylcobalamin at 1.75 and 2.0 A resolution, respectively. This monomeric, allosterically regulated class II RNR retains all the key structural features associated with the catalytic and regulatory machinery of oligomeric RNRs. Surprisingly, the dimer interface responsible for effector binding in class I RNR is preserved through a single 130-residue insertion in the class II structure. Thus, L. leichmannii RNR is a paradigm for the simplest structural entity capable of ribonucleotide reduction, a reaction linking the RNA and DNA worlds.

PubMed: 11875520
DOI: 10.1038/nsb774

実験手法

X-RAY DIFFRACTION (1.75 Å)