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This Sandbox is Reserved from January through July 31, 2018 for use in the course HLSC322: Principles of Genetics and Genomics taught by Genevieve Houston-Ludlam at the University of Maryland, College Park, USA. This reservation includes Sandbox Reserved 1311 through Sandbox Reserved 1430.

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Contents 1 Nitrogenase 2 Structural Highlights 3 Fe-ATP Complex 4 References

Nitrogenase

spinqualitylabelsall models Structure of Nitrogenase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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Structural Highlights

The structure of nitrogenase consists of metal clusters centered throughout the protein. Three of these clusters are the 4Fe-4S Cluster, P-Cluster, and FeMo-Cluster. At either end of the protein are two copies of the Fe protein dimer, which is also the site of the ATP binding site. At these sites are ADP molecules which form a stable complex with the Fe protein. The MoFe protein, the central components of the protein, is where most of nitrogenase’s function is carried out. This protein requires a constant state of electrons which is supplied by the Fe protein which uses the hydrolysis of ATP to pump these electrons into the MoFe protein. Thus, it is helpful for the Fe protein to be coupled with ADP/ATP at the ends of the protein.

Fe-ATP Complex

spinqualitylabelsall models Escherichia coli reca protein-bound DNA (PDB entry 3rec) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Disease Relevance

References

Goodsell, David. “Nitrogenase.” PDB-101: Nitrogenase, Protein Data Bank, Feb. 2002, pdb101.rcsb.org/motm/26.