6EFV
The NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation that is unique to this diflavin reductase
Summary for 6EFV
| Entry DOI | 10.2210/pdb6efv/pdb |
| Descriptor | Sulfite reductase [NADPH] flavoprotein alpha-component, FLAVIN-ADENINE DINUCLEOTIDE, FLAVIN MONONUCLEOTIDE, ... (6 entities in total) |
| Functional Keywords | sulfite reductase, sulfite reductase flavoprotein, cytochrome p450 reductase, fad, fmn, electron transfer, flavoprotein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 65868.06 |
| Authors | Tavolieri, A.M.,Askenasy, I.,Murray, D.T.,Pennington, J.M.,Stroupe, M.E. (deposition date: 2018-08-17, release date: 2019-02-27, Last modification date: 2023-10-11) |
| Primary citation | Tavolieri, A.M.,Murray, D.T.,Askenasy, I.,Pennington, J.M.,McGarry, L.,Stanley, C.B.,Stroupe, M.E. NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation unique to this diflavin reductase. J. Struct. Biol., 205:170-179, 2019 Cited by PubMed Abstract: This is the first X-ray crystal structure of the monomeric form of sulfite reductase (SiR) flavoprotein (SiRFP-60) that shows the relationship between its major domains in an extended position not seen before in any homologous diflavin reductases. Small angle neutron scattering confirms this novel domain orientation also occurs in solution. Activity measurements of SiR and SiRFP variants allow us to propose a novel mechanism for electron transfer from the SiRFP reductase subunit to its oxidase metalloenzyme partner that, together, make up the SiR holoenzyme. Specifically, we propose that SiR performs its 6-electron reduction via intramolecular or intermolecular electron transfer. Our model explains both the significance of the stoichiometric mismatch between reductase and oxidase subunits in the holoenzyme and how SiR can handle such a large volume electron reduction reaction that is at the heart of the sulfur bio-geo cycle. PubMed: 30654136DOI: 10.1016/j.jsb.2019.01.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.341 Å) |
Structure validation
Download full validation report
