1JNZ
Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6 resolution
Summary for 1JNZ
| Entry DOI | 10.2210/pdb1jnz/pdb |
| Related | 1JNR |
| Descriptor | adenylylsulfate reductase, SULFITE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (6 entities in total) |
| Functional Keywords | sulfur metabolism, adenylylsulfate reductase, iron-sulfur flavoprotein, catalysis, oxidoreductase |
| Biological source | Archaeoglobus fulgidus DSM 4304 More |
| Total number of polymer chains | 4 |
| Total formula weight | 183742.32 |
| Authors | Fritz, G.,Roth, A.,Schiffer, A.,Buechert, T.,Bourenkov, G.,Bartunik, H.D.,Huber, H.,Stetter, K.O.,Kroneck, P.M.,Ermler, U. (deposition date: 2001-07-26, release date: 2002-03-27, Last modification date: 2023-08-16) |
| Primary citation | Fritz, G.,Roth, A.,Schiffer, A.,Buchert, T.,Bourenkov, G.,Bartunik, H.D.,Huber, H.,Stetter, K.O.,Kroneck, P.M.,Ermler, U. Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-A resolution Proc.Natl.Acad.Sci.USA, 99:1836-1841, 2002 Cited by PubMed Abstract: The iron-sulfur flavoenzyme adenylylsulfate (adenosine 5'-phosphosulfate, APS) reductase catalyzes reversibly the reduction of APS to sulfite and AMP. The structures of APS reductase from the hyperthermophilic Archaeoglobus fulgidus in the two-electron reduced state and with sulfite bound to FAD are reported at 1.6- and 2.5- resolution, respectively. The FAD-sulfite adduct was detected after soaking the crystals with APS. This finding and the architecture of the active site strongly suggest that catalysis involves a nucleophilic attack of the N5 atom of reduced FAD on the sulfur atom of APS. In view of the high degree of similarity between APS reductase and fumarate reductase especially with regard to the FAD-binding alpha-subunit, it is proposed that both subunits originate from a common ancestor resembling archaeal APS reductase. The two electrons required for APS reduction are transferred via two [4Fe-4S] clusters from the surface of the protein to FAD. The exceptionally large difference in reduction potential of these clusters (-60 and -500 mV) can be explained by interactions of the clusters with the protein matrix. PubMed: 11842205DOI: 10.1073/pnas.042664399 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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