Sandbox Reserved 1063: Difference between revisions
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=== Hydrogen Bond Network === | === Hydrogen Bond Network === | ||
The binding of zinc metals creates a hydrogen bond network within the protein that connects the metal binding sites and the [https://en.wikipedia.org/wiki/DNA-binding_domain DNA binding domain]. The <scene name='69/694230/Hydrogen_bonding_1/5'>hydrogen bond network</scene> (<scene name='69/694230/Hydrogen_bonding_2/5'>with measurements</scene>) (residues in stick structures, colored by atom type) is characteristic of the MarR family as a whole and connects the metal binding pockets to the α4 helix also known as the DNA recognition helix. <scene name='69/694230/Recognition_helix/3'>Several residues</scene> in this helix recognize the DNA ligand | The binding of zinc metals creates a hydrogen bond network within the protein that connects the metal binding sites and the [https://en.wikipedia.org/wiki/DNA-binding_domain DNA binding domain]. The <scene name='69/694230/Hydrogen_bonding_1/5'>hydrogen bond network</scene> (<scene name='69/694230/Hydrogen_bonding_2/5'>with measurements</scene>) (residues in stick structures, colored by atom type) is characteristic of the MarR family as a whole and connects the metal binding pockets to the α4 helix also known as the DNA recognition helix. <scene name='69/694230/Recognition_helix/3'>Several residues</scene> in this helix recognize the DNA ligand. The hydrogen bond network connects the α2 and α4 helices via hydrogen bonding between specific residues. After zinc is bound, a glutamate (E24) residue from a random coil accepts a hydrogen bond from the carboxamide end of an asparagine (N38) residue from the α2 helix. A glutamine (Q40) residue from α2 helix accepts a hydrogen bond from a serine (S74) residue from the α4 helix <ref name="guerra" />. | ||
[[Image:H Bonding of DNA.png|300 px|left|thumb|'''Figure 4'''. The Hydrogen Bonding Network is shown with dotted green lines approximately 2.8 angstroms between residues.]] | [[Image:H Bonding of DNA.png|300 px|left|thumb|'''Figure 4'''. The Hydrogen Bonding Network is shown with dotted green lines approximately 2.8 angstroms between residues.]] | ||
== ''' | == '''Clinical Relevance''' == | ||
Streptococcus pneumoniae, the host to AdcR, is a significant pathogenic bacterium. Although asymptomatic in healthy individuals, S. pneumoniae can lead to Bronchitis, meningitis conjunctivitis, or brain abscesses in those with weaker immune systems. Host regulation of zinc is often used to combat pathogens such as S. pneumoniae <ref name="Sanson" />. A better understanding of AdcR, the regulator that controls the transcription of zinc specific uptake transporters, could help to illuminate better mechanism for combating not only S. pneumoniae, but other comparable bacteria. | Streptococcus pneumoniae, the host to AdcR, is a significant pathogenic bacterium. Although asymptomatic in healthy individuals, S. pneumoniae can lead to Bronchitis, meningitis conjunctivitis, or brain abscesses in those with weaker immune systems. Host regulation of zinc is often used to combat pathogens such as S. pneumoniae <ref name="Sanson" />. A better understanding of AdcR, the regulator that controls the transcription of zinc specific uptake transporters, could help to illuminate better mechanism for combating not only S. pneumoniae, but other comparable bacteria. | ||
