4BMU

Crystal Structure of Ribonucleotide Reductase di-manganese(II) NrdF from Bacillus cereus

4BMU の概要

• エントリーDOI: 10.2210/pdb4bmu/pdb
• 関連するPDBエントリー: 4BMQ 4BMR 4BMT
• 分子名称: RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT BETA, MANGANESE (II) ION (3 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: BACILLUS CEREUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74325.72

構造登録者

Hersleth, H.-P.,Tomter, A.B.,Hammerstad, M.,Rohr, A.K.,Andersson, K.K. (登録日: 2013-05-10, 公開日: 2014-03-19, 最終更新日: 2023-12-20)

主引用文献

Hammerstad, M.,Hersleth, H.,Tomter, A.B.,Rohr, A.K.,Andersson, K.K.
Crystal Structure of Bacillus Cereus Class Ib Ribonucleotide Reductase Di-Iron Nrdf in Complex with Nrdi.
Acs Chem.Biol., 9:526-, 2014

PubMed Abstract: Class Ib ribonucleotide reductases (RNRs) use a dimetal-tyrosyl radical (Y•) cofactor in their NrdF (β2) subunit to initiate ribonucleotide reduction in the NrdE (α2) subunit. Contrary to the diferric tyrosyl radical (Fe(III)2-Y•) cofactor, which can self-assemble from Fe(II)2-NrdF and O2, generation of the Mn(III)2-Y• cofactor requires the reduced form of a flavoprotein, NrdIhq, and O2 for its assembly. Here we report the 1.8 Å resolution crystal structure of Bacillus cereus Fe2-NrdF in complex with NrdI. Compared to the previously solved Escherichia coli NrdI-Mn(II)2-NrdF structure, NrdI and NrdF binds similarly in Bacillus cereus through conserved core interactions. This protein-protein association seems to be unaffected by metal ion type bound in the NrdF subunit. The Bacillus cereus Mn(II)2-NrdF and Fe2-NrdF structures, also presented here, show conformational flexibility of residues surrounding the NrdF metal ion site. The movement of one of the metal-coordinating carboxylates is linked to the metal type present at the dimetal site and not associated with NrdI-NrdF binding. This carboxylate conformation seems to be vital for the water network connecting the NrdF dimetal site and the flavin in NrdI. From these observations, we suggest that metal-dependent variations in carboxylate coordination geometries are important for active Y• cofactor generation in class Ib RNRs. Additionally, we show that binding of NrdI to NrdF would structurally interfere with the suggested α2β2 (NrdE-NrdF) holoenzyme formation, suggesting the potential requirement for NrdI dissociation before NrdE-NrdF assembly after NrdI-activation. The mode of interactions between the proteins involved in the class Ib RNR system is, however, not fully resolved.

PubMed: 24295378
DOI: 10.1021/CB400757H

実験手法

X-RAY DIFFRACTION (1.9 Å)