6bbl | pdb_00006bbl

Crystal structure of the a-96Gln MoFe protein variant in the presence of the substrate acetylene

spinqualitylabelsall models 6bbl, resolution 1.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6bbl is a 4 chain structure with sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1CL, C2H, FE, HCA, ICS, IMD, MG Activity: Nitrogenase, with EC number 1.18.6.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NIFD_AZOVI] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. [NIFK_AZOVI] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. Publication Abstract from PubMed The biological reduction of dinitrogen (N2) to ammonia is catalyzed by the complex metalloenzyme nitrogenase. Structures of the nitrogenase component proteins, Iron (Fe) protein and Molybdenumiron (MoFe) protein, and the stabilized complexes these component proteins, have been determined, providing a foundation for a number of fundamental aspects of the complicated catalytic mechanism. The reduction of dinitrogen to ammonia is a complex process that involves the binding of N2 followed by reduction with multiple electrons and protons. Electron transfer into nitrogenase is typically constrained to the unique electron donor, the Fe protein. These constraints have prevented structural characterization of the active site with bound substrate. Recently it has been realized that selected amino acid substitutions in the environment of the active site metal cluster (Ironmolybdenum cofactor, FeMo-co) allow substrates to persist even in the resting state. Reported here is a 1.70A crystal structure of a nitrogenase MoFe protein alpha-96(ArgGln) variant with the alternative substrate acetylene trapped in a channel in close proximity to FeMo-co. Complementary theoretical calculations support the validity of the acetylene interaction at this site and is also consistent with more favorable interactions in the variant MoFe protein compared to the native MoFe protein. This work represents the first structural evidence of a substrate trapped in the nitrogenase MoFe protein and is consistent with earlier assignments of proposed substrate pathways and substrate binding sites deduced from biochemical, spectroscopic, and theoretical studies. Structural characterization of the nitrogenase molybdenum-iron protein with the substrate acetylene trapped near the active site.,Keable SM, Vertemara J, Zadvornyy OA, Eilers BJ, Danyal K, Rasmussen AJ, De Gioia L, Zampella G, Seefeldt LC, Peters JW J Inorg Biochem. 2017 Dec 13;180:129-134. doi: 10.1016/j.jinorgbio.2017.12.008. PMID:29275221 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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