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Related Concept Videos

Overview of Nitrogen Metabolism01:20

Overview of Nitrogen Metabolism

Nitrogen is a very important element for life because it is a major constituent of proteins and nucleic acids. It is a macronutrient, and in nature, it is recycled from organic compounds and stored in the form of  ammonia, ammonium ions, nitrate, nitrite, or  nitrogen gas by many metabolic processes. Many of these metabolic processes are carried out only by prokaryotes.
The largest pool of nitrogen available in the terrestrial ecosystem is gaseous nitrogen (N2) from the air, but this nitrogen...
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Nitrogen is an essential element in biological systems, forming a crucial component of proteins, nucleic acids, and other cellular constituents. Many bacteria and archaea acquire nitrogen in the form of nitrate (NO₃⁻) or ammonia (NH₃), which are then assimilated into biomolecules through specific enzymatic pathways.Assimilatory Nitrate ReductionWhen nitrate enters the cell, it undergoes a two-step reduction process known as assimilatory nitrate reduction. Initially, the enzyme nitrate reductase...
Amino acids03:42

Amino acids

Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
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The urea cycle describes how liver cells convert ammonia to urea. Ammonia is a toxic waste product of protein catabolism. Land animals must convert ammonia into the less toxic urea which can be safely eliminated by the kidneys through urine. Marine animals excrete ammonia directly, and the surrounding water dilutes the ammonia to safe levels.
Cell Inclusions01:27

Cell Inclusions

Prokaryotic cells possess a variety of inclusions that play crucial roles in nutrient storage, metabolic processes, and environmental adaptation. These structures enable bacteria to thrive under fluctuating environmental conditions by storing essential resources and optimizing their metabolic efficiency.Carbon Storage: Poly-β-Hydroxybutyric Acid and Glycogen GranulesBacteria frequently store excess carbon in specialized granules. Poly-β-hydroxybutyric acid (PHB) granules are lipid polymers that...
Comparative Excretory Systems02:24

Comparative Excretory Systems

Animals have evolved different strategies for excretion, the removal of waste from the body. Most waste must be dissolved in water to be excreted, so an animal’s excretory strategy directly affects its water balance.

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Workflow Based on the Combination of Isotopic Tracer Experiments to Investigate Microbial Metabolism of Multiple Nutrient Sources
12:47

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Published on: January 22, 2018

Arginine and nitrogen storage.

José L Llácer1, Ignacio Fita, Vicente Rubio

  • 1Instituto de Biomedicina de Valencia-Consejo Superior de Investigaciones Cientificas (IBV-CSIC) and Centro de Investigación Biomédica en Red de Enfermedades Raras (CIBERER-ISCIII), Jaime Roig 11, Valencia 46010, Spain.

Current Opinion in Structural Biology
|November 18, 2008
PubMed
Summary

The PII protein regulates arginine synthesis in organisms by binding to N-acetylglutamate kinase (NAGK). This interaction, detailed by crystal structures, controls nitrogen storage in response to nutrient availability.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Nitrogen metabolism is crucial for all organisms.
  • Photosynthetic organisms store excess nitrogen as arginine when abundant.
  • N-acetylglutamate kinase (NAGK) controls arginine biosynthesis and is regulated by feedback inhibition.

Purpose of the Study:

  • To elucidate the molecular mechanism of NAGK regulation by the PII signaling protein.
  • To understand how PII binding relieves feedback inhibition of NAGK.
  • To provide structural insights into the PII-NAGK complex.

Main Methods:

  • X-ray crystallography was used to determine the structures of NAGK, PII proteins, and their complexes.
  • Structural analysis focused on the interaction interface between PII and NAGK.

Main Results:

  • Crystal structures revealed a complex where two PII trimers sandwich a NAGK hexamer.
  • Each PII subunit interacts with a NAGK subunit, causing a conformational change in NAGK.
  • This interaction leads to a narrowing of the NAGK ring and a low-affinity conformation of arginine-binding sites, relieving feedback inhibition.

Conclusions:

  • The PII protein acts as a sensor and regulator of arginine biosynthesis by directly interacting with NAGK.
  • Structural data reveals the mechanism of feedback inhibition relief, crucial for nitrogen storage.
  • This study provides a molecular basis for understanding nitrogen homeostasis in prokaryotic and eukaryotic photosynthetic organisms.