4Z7C
Diphosphomevalonate decarboxylase from the Sulfolobus solfataricus, space group h32
Summary for 4Z7C
| Entry DOI | 10.2210/pdb4z7c/pdb |
| Related | 4Z7D 4Z7Y |
| Descriptor | Diphosphomevalonate decarboxylase, PHOSPHATE ION, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | diphosphomevalonate decarboxylase, sulfolobus solfataricus, disulfide bond, thermostability, lyase |
| Biological source | Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) |
| Total number of polymer chains | 1 |
| Total formula weight | 37253.38 |
| Authors | Unno, H.,Hattori, A.,Hemmi, H. (deposition date: 2015-04-07, release date: 2015-09-16, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 26303832DOI: 10.1128/JB.00352-15 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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