2bih | pdb_00002bih

CRYSTAL STRUCTURE OF THE MOLYBDENUM-CONTAINING NITRATE REDUCING FRAGMENT OF PICHIA ANGUSTA ASSIMILATORY NITRATE REDUCTASE

spinqualitylabelsall models 2bih, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2bih is a 1 chain structure with sequence from Ogataea angusta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MTV Related: 2bii Activity: Nitrate reductase (NAD(P)H), with EC number 1.7.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Nitrate assimilation in autotrophs provides most of the reduced nitrogen on earth. In eukaryotes, reduction of nitrate to nitrite is catalyzed by the molybdenum-containing NAD(P)H:nitrate reductase (NR; EC 1.7.1.1-3). In addition to the molybdenum center, NR contains iron-heme and flavin adenine dinucleotide as redox cofactors involved in an internal electron transport chain from NAD(P)H to nitrate. Recombinant, catalytically active Pichia angusta nitrate-reducing, molybdenum-containing fragment (NR-Mo) was expressed in P. pastoris and purified. Crystal structures for NR-Mo were determined at 1.7 and 2.6 angstroms. These structures revealed a unique slot for binding nitrate in the active site and identified key Arg and Trp residues potentially involved in nitrate binding. Dimeric NR-Mo is similar in overall structure to sulfite oxidases, with significant differences in the active site. Sulfate bound in the active site caused conformational changes, as compared with the unbound enzyme. Four ordered water molecules located in close proximity to Mo define a nitrate binding site, a penta-coordinated reaction intermediate, and product release. Because yeast NAD(P)H:NR is representative of the family of eukaryotic NR, we propose a general mechanism for nitrate reduction catalysis. Structural basis of eukaryotic nitrate reduction: crystal structures of the nitrate reductase active site.,Fischer K, Barbier GG, Hecht HJ, Mendel RR, Campbell WH, Schwarz G Plant Cell. 2005 Apr;17(4):1167-79. Epub 2005 Mar 16. PMID:15772287 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nitrate reductase

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