6efv

The NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation that is unique to this diflavin reductase

spinqualitylabelsall models 6efv, resolution 2.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6efv is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.341Å Ligands: CXS, FAD, FMN, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function W8SX42_ECOLX Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.[HAMAP-Rule:MF_01541][PIRNR:PIRNR000207][SAAS:SAAS00040600] Publication Abstract from PubMed 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. NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation unique to this diflavin reductase.,Tavolieri AM, Murray DT, Askenasy I, Pennington JM, McGarry L, Stanley CB, Stroupe ME J Struct Biol. 2019 Feb 1;205(2):170-179. doi: 10.1016/j.jsb.2019.01.001. Epub, 2019 Jan 15. PMID:30654136 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA