3wi9

Crystal structure of copper nitrite reductase from Geobacillus kaustophilus

spinqualitylabelsall models 3wi9, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wi9 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACY, CU, MPD, NA, SO4, ZN Related: 3wia Activity: Nitrite reductase (NO-forming), with EC number 1.7.2.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The crystal structures of copper-containing nitrite reductase (CuNiR) from the thermophilic Gram-positive bacterium Geobacillus kaustophilus HTA426 and the amino (N)-terminal 68 residue-deleted mutant were determined at resolutions of 1.3A and 1.8A, respectively. Both structures show a striking resemblance with the overall structure of the well-known CuNiRs composed of two Greek key beta-barrel domains; however, a remarkable structural difference was found in the N-terminal region. The unique region has one beta-strand and one alpha-helix extended to the northern surface of the type-1 copper site. The superposition of the Geobacillus CuNiR model on the electron-transfer complex structure of CuNiR with the redox partner cytochrome c551 in other denitrifier system led us to infer that this region contributes to the transient binding with the partner protein during the interprotein electron transfer reaction in the Geobacillus system. Furthermore, electron-transfer kinetics experiments using N-terminal residue-deleted mutant and the redox partner, Geobacillus cytochrome c551, were carried out. These structural and kinetics studies demonstrate that the region is directly involved in the specific partner recognition. Structural and functional characterization of the Geobacillus copper nitrite reductase: involvement of the unique N-terminal region in the interprotein electron transfer with its redox partner.,Fukuda Y, Koteishi H, Yoneda R, Tamada T, Takami H, Inoue T, Nojiri M Biochim Biophys Acta. 2014 Mar;1837(3):396-405. doi:, 10.1016/j.bbabio.2014.01.004. Epub 2014 Jan 14. PMID:24440558 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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