Sandbox Reserved 1347
From Proteopedia
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== Structural Highlights == | == Structural Highlights == | ||
| - | The structure of nitrogenase consists of metal clusters centered throughout the protein. Three of these clusters are the <scene name='77/777667/Fe4s4_cluster/3'>4Fe-4S Cluster</scene>, <scene name='77/777667/P-cluster/4'>P-cluster</scene>, and M-Cluster (MoFe-cluster). At either end of the protein, there are also 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 the 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. | + | The structure of nitrogenase consists of metal clusters centered throughout the protein. Three of these clusters are the <scene name='77/777667/Fe4s4_cluster/3'>4Fe-4S Cluster</scene>, <scene name='77/777667/P-cluster/4'>P-cluster</scene>, and <scene name='77/777667/M-cluster/2'>M-Cluster</scene> (MoFe-cluster). At either end of the protein, there are also 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 the 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. |
== Function == | == Function == | ||
Revision as of 19:43, 28 February 2018
| 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 |
Nitrogenase
Nitrogen is needed by all living things to build proteins and nucleic acids. Nitrogen gas is stable due to its triple bond structure and is thus hard to break apart into individual molecules of Nitrogen. Often, the growth of plants is limited by the amount of nitrogen available in the soil. Small amounts of usable forms of nitrogen are formed by lightning and the ultraviolet light from the sun. Significant amounts of nitrogen are fed to plants in the form of industrial fertilizers. But the majority of usable nitrogen comes from the ability to break it down by bacteria using the enzyme Nitrogenase.
Structural Highlights
The structure of nitrogenase consists of metal clusters centered throughout the protein. Three of these clusters are the , , and (MoFe-cluster). At either end of the protein, there are also 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 the 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.
Function
Nitrogen Fixation
Nitrogen fixation allows bacteria to convert nitrogen gas into ammonia, which can be used to form proteins and nucleic acids. The enzyme nitrogenase in bacteria primarily drives this reaction with high quantities of ATP, metal ions, and the molybdenum ion.
Relevance
</StructureSection>
References
Goodsell, David. “Nitrogenase.” PDB-101: Nitrogenase, Protein Data Bank, Feb. 2002, pdb101.rcsb.org/motm/26.
