4Z7C

Diphosphomevalonate decarboxylase from the Sulfolobus solfataricus, space group h32

4Z7C の概要

• エントリーDOI: 10.2210/pdb4z7c/pdb
• 関連するPDBエントリー: 4Z7D 4Z7Y
• 分子名称: Diphosphomevalonate decarboxylase, PHOSPHATE ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: diphosphomevalonate decarboxylase, sulfolobus solfataricus, disulfide bond, thermostability, lyase
• 由来する生物種: Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37253.38

構造登録者

Unno, H.,Hattori, A.,Hemmi, H. (登録日: 2015-04-07, 公開日: 2015-09-16, 最終更新日: 2024-10-30)

主引用文献

Hattori, A.,Unno, H.,Goda, S.,Motoyama, K.,Yoshimura, T.,Hemmi, H.
In Vivo Formation of the Protein Disulfide Bond That Enhances the Thermostability of Diphosphomevalonate Decarboxylase, an Intracellular Enzyme from the Hyperthermophilic Archaeon Sulfolobus solfataricus
J.Bacteriol., 197:3463-3471, 2015

PubMed Abstract: In the present study, the crystal structure of recombinant diphosphomevalonate decarboxylase from the hyperthermophilic archaeon Sulfolobus solfataricus was solved as the first example of an archaeal and thermophile-derived diphosphomevalonate decarboxylase. The enzyme forms a homodimer, as expected for most eukaryotic and bacterial orthologs. Interestingly, the subunits of the homodimer are connected via an intersubunit disulfide bond, which presumably formed during the purification process of the recombinant enzyme expressed in Escherichia coli. When mutagenesis replaced the disulfide-forming cysteine residue with serine, however, the thermostability of the enzyme was significantly lowered. In the presence of β-mercaptoethanol at a concentration where the disulfide bond was completely reduced, the wild-type enzyme was less stable to heat. Moreover, Western blot analysis combined with nonreducing SDS-PAGE of the whole cells of S. solfataricus proved that the disulfide bond was predominantly formed in the cells. These results suggest that the disulfide bond is required for the cytosolic enzyme to acquire further thermostability and to exert activity at the growth temperature of S. solfataricus.

PubMed: 26303832
DOI: 10.1128/JB.00352-15

実験手法

X-RAY DIFFRACTION (2.2 Å)