3ml1

Crystal Structure of the Periplasmic Nitrate Reductase from Cupriavidus necator

spinqualitylabelsall models 3ml1, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ml1 is a 2 chain structure with sequence from Cupriavidus necator H16. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: HEC, MGD, MOS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NAPB_CUPNH Electron transfer subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from the membrane-anchored tetraheme c-type NapC protein and transfers these to NapA subunit, thus allowing electron flow between membrane and periplasm. Essential for periplasmic nitrate reduction with nitrate as the terminal electron acceptor. Publication Abstract from PubMed The periplasmic nitrate reductase (NapAB) from Cupriavidus necator is a heterodimeric protein that belongs to the dimethyl sulfoxide reductase family of mononuclear Mo-containing enzymes and catalyzes the reduction of nitrate to nitrite. The protein comprises a large catalytic subunit (NapA, 91 kDa) containing the molybdenum active site plus one [4Fe-4S] cluster, as well as a small subunit (NapB, 17 kDa), which is a diheme c-type cytochrome involved in electron transfer. Crystals of the oxidized form of the enzyme diffracted beyond 1.5 A at the European Synchrotron Radiation Facility. This is the highest resolution reported to date for a nitrate reductase, providing true atomic details of the protein active center, and this showed further evidence on the molybdenum coordination sphere, corroborating previous data on the related Desulfovibrio desulfuricans NapA. The molybdenum atom is bound to a total of six sulfur atoms, with no oxygen ligands or water molecules in the vicinity. In the present work, we were also able to prepare partially reduced crystals that revealed two alternate conformations of the Mo-coordinating cysteine. This crystal form was obtained by soaking dithionite into crystals grown in the presence of the ionic liquid [C(4)mim]Cl(-). In addition, UV-Vis and EPR spectroscopy studies showed that the periplasmic nitrate reductase from C. necator might work at unexpectedly high redox potentials when compared to all periplasmic nitrate reductases studied to date. The Crystal Structure of Cupriavidus necator Nitrate Reductase in Oxidized and Partially Reduced States.,Coelho C, Gonzalez PJ, Moura JJ, Moura I, Trincao J, Joao Romao M J Mol Biol. 2011 Mar 23. PMID:21419779 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome C 3D structures Nitrate reductase

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