Sandbox ggc8

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== ''narG'' Nitrogen reductase ==
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== ''narG'' Nitrate reductase ==
<StructureSection load='3IR7' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='3IR7' size='340' side='right' caption='Caption for this structure' scene=''>
<scene name='75/752272/N_to_c_rainbow/1'>narG 3IR7 mutant</scene>
<scene name='75/752272/N_to_c_rainbow/1'>narG 3IR7 mutant</scene>
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== Function ==
== Function ==
Nitrate reductase plays a strong role in the nitrogen cycle. It fixes nitrate to nitrite so it can be more easily converted to nitrogen gas for the environment. <ref>DOI:
Nitrate reductase plays a strong role in the nitrogen cycle. It fixes nitrate to nitrite so it can be more easily converted to nitrogen gas for the environment. <ref>DOI:
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10.1146/annurev.arplant.50.1.277</ref> Nitrate reduction can also cause increases in the levels of phosphate in groundwater. <ref>doi:10.1007/s10533-009-9387-8</ref> ''narG'' consists of 3 sub-units; G, H, and I. The G sub-unit contains the active site of ''narG'' while the other sub-units are involved in electron transport.
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10.1146/annurev.arplant.50.1.277</ref> Nitrate reduction can also cause increases in the levels of phosphate in groundwater. <ref>doi:10.1007/s10533-009-9387-8</ref> ''narG'' consists of 3 sub-units; G, H, and I. The G sub-unit contains the active site of ''narG'' while the other sub-units are involved in electron transport. The I sub-unit is also a membrane anchor protein. <ref>doi: 10.1074/jbc.M109.066027</ref>
== Relevance ==
== Relevance ==
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== Structural highlights ==
== Structural highlights ==
<scene name='75/752272/Narg_active_site/2'>Active site of narG</scene> in the G sub-unit, where nitrate is fixed to nitrite. The molybdenum molecule is responsible for nitrate reduction. The FS0 cluster is a potential electron transfer route for the molybdenum core. <ref>doi: 10.1074/jbc.M109.066027</ref>
<scene name='75/752272/Narg_active_site/2'>Active site of narG</scene> in the G sub-unit, where nitrate is fixed to nitrite. The molybdenum molecule is responsible for nitrate reduction. The FS0 cluster is a potential electron transfer route for the molybdenum core. <ref>doi: 10.1074/jbc.M109.066027</ref>
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Molecules involved in <scene name='75/752272/Electron_transport/1'>electron transportation</scene> are highlighted. The molecules involved include 3 heme groups and 5 iron-sulfur complexes. This electron transport chain helps maintain molybdenum's ability to fix nitrate. <ref>doi: 10.1074/jbc.M109.066027</ref>
<scene name='75/752272/His_residue/1'>His residue</scene> where mutations can occur that prevent the FS0 cluster from binding, specifically a mutation to <scene name='75/752272/3ir6_mutant/1'>Serine</scene>.
<scene name='75/752272/His_residue/1'>His residue</scene> where mutations can occur that prevent the FS0 cluster from binding, specifically a mutation to <scene name='75/752272/3ir6_mutant/1'>Serine</scene>.
<scene name='75/752272/Ser_residue/1'>Arg residue</scene> has been mutated to a Serine. This can reduce enzyme efficiency by removal of the positive charge of Arginine.
<scene name='75/752272/Ser_residue/1'>Arg residue</scene> has been mutated to a Serine. This can reduce enzyme efficiency by removal of the positive charge of Arginine.
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Molecules involved in <scene name='75/752272/Electron_transport/1'>electron transportation</scene> are highlighted. The molecules involved include 3 heme groups and 5 iron-sulfur complexes. This electron transport chain helps maintain molybdenum's ability to fix nitrate.
 

Current revision

narG Nitrate reductase

Caption for this structure

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References

  1. Campbell WH. NITRATE REDUCTASE STRUCTURE, FUNCTION AND REGULATION: Bridging the Gap between Biochemistry and Physiology. Annu Rev Plant Physiol Plant Mol Biol. 1999 Jun;50:277-303. PMID:15012211 doi:http://dx.doi.org/10.1146/annurev.arplant.50.1.277
  2. doi: https://dx.doi.org/10.1007/s10533-009-9387-8
  3. Rothery RA, Bertero MG, Spreter T, Bouromand N, Strynadka NC, Weiner JH. Protein crystallography reveals a role for the FS0 cluster of Escherichia coli nitrate reductase A (NarGHI) in enzyme maturation. J Biol Chem. 2010 Mar 19;285(12):8801-7. Epub 2010 Jan 6. PMID:20053990 doi:10.1074/jbc.M109.066027
  4. doi: https://dx.doi.org/10.1007/s10533-009-9387-8
  5. Rothery RA, Bertero MG, Spreter T, Bouromand N, Strynadka NC, Weiner JH. Protein crystallography reveals a role for the FS0 cluster of Escherichia coli nitrate reductase A (NarGHI) in enzyme maturation. J Biol Chem. 2010 Mar 19;285(12):8801-7. Epub 2010 Jan 6. PMID:20053990 doi:10.1074/jbc.M109.066027
  6. Rothery RA, Bertero MG, Spreter T, Bouromand N, Strynadka NC, Weiner JH. Protein crystallography reveals a role for the FS0 cluster of Escherichia coli nitrate reductase A (NarGHI) in enzyme maturation. J Biol Chem. 2010 Mar 19;285(12):8801-7. Epub 2010 Jan 6. PMID:20053990 doi:10.1074/jbc.M109.066027
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