Sandbox Reserved 1070: Difference between revisions
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The opposite side of the protein has a small cluster of conserved residues <scene name='69/698113/Conserved_surface_residues/ | The opposite side of the protein has a small cluster of conserved residues <scene name='69/698113/Conserved_surface_residues/7'>Tyrosine-149, Glutamine-208, and Tryptophan-225</scene>. | ||
[[Image:Final_Surface_Web_Logo.PNG |625× 121px|thumb|left|Four strictly conserved residues of five known functional MgtC orthologs of the soluble C-terminal domain. The figure was prepared using WebLogo. (http://weblogo.berkeley.edu/)]] | [[Image:Final_Surface_Web_Logo.PNG |625× 121px|thumb|left|Four strictly conserved residues of five known functional MgtC orthologs of the soluble C-terminal domain. The figure was prepared using WebLogo. (http://weblogo.berkeley.edu/)]] | ||
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===Potential for Binding Amino Acids=== | ===Potential for Binding Amino Acids=== | ||
The exploration of this role for MgtC was first considered because of the ACT domain-like structure of the C-terminal domain. | The exploration of this role for MgtC was first considered because of the ACT domain-like structure of the C-terminal domain. | ||
ACT domains commonly bind small amino acids within the cell as a form of [http://geneontology.org/page/regulation regulation]. Yang ''et al''. showed that the structure of the C-terminal domain overlaps significantly with the structure of [http://proteopedia.org/wiki/index.php/1psd SerA] (PDB: [http://www.rcsb.org/pdb/explore/explore.do?structureId=1psd 1PSD]), a known amino acid-binding ACT domain from ''[http://www.cdc.gov/ecoli/ E. coli]''. '''Figure 1A''' shows the overlap of these two proteins; the cyan protein represents MgtC and the orange protein represents SerA. However, the glycine that is critical for the binding of amino acids in these ACT domains has been substituted in MgtC with a <scene name='69/698113/Sub_residues_of_sera/ | ACT domains commonly bind small amino acids within the cell as a form of [http://geneontology.org/page/regulation regulation]. Yang ''et al''. showed that the structure of the C-terminal domain overlaps significantly with the structure of [http://proteopedia.org/wiki/index.php/1psd SerA] (PDB: [http://www.rcsb.org/pdb/explore/explore.do?structureId=1psd 1PSD]), a known amino acid-binding ACT domain from ''[http://www.cdc.gov/ecoli/ E. coli]''. '''Figure 1A''' shows the overlap of these two proteins; the cyan protein represents MgtC and the orange protein represents SerA. However, the glycine that is critical for the binding of amino acids in these ACT domains has been substituted in MgtC with a <scene name='69/698113/Sub_residues_of_sera/3'>tyrosine</scene>, likely abolishing any potential amino acid binding activity <ref name="mgtc"/> | ||
===Potential for Chelation=== | ===Potential for Chelation=== | ||
As with the potential for binding amino acids, this role was also explored because of the structural similarity of the C-terminal domain with ACT domains, as ACT domains also serve as excellent [http://en.wikipedia.org/wiki/Chelation chelators] to sequester cations within the cell. Yang ''et al''. also compared the structure of the C-terminal domain of MgtC with an ACT domain of a known chelator, [http://proteopedia.org/wiki/index.php/3lgh NikR] (PDB: [http://www.rcsb.org/pdb/explore/explore.do?structureId=3LGH 3LGH]). These structures overlapped quite well, indicating that MgtC may serve as a chelator. '''Figure 1B''' highlights the significant overlap between these residues; the cyan protein represents MgtC and the orange protein represents NikR. However, the two histidine residues and the cysteine residue present in NikR that serve as the chelating residues are modified to <scene name='69/698113/Sub_residues_of_chelat/ | As with the potential for binding amino acids, this role was also explored because of the structural similarity of the C-terminal domain with ACT domains, as ACT domains also serve as excellent [http://en.wikipedia.org/wiki/Chelation chelators] to sequester cations within the cell. Yang ''et al''. also compared the structure of the C-terminal domain of MgtC with an ACT domain of a known chelator, [http://proteopedia.org/wiki/index.php/3lgh NikR] (PDB: [http://www.rcsb.org/pdb/explore/explore.do?structureId=3LGH 3LGH]). These structures overlapped quite well, indicating that MgtC may serve as a chelator. '''Figure 1B''' highlights the significant overlap between these residues; the cyan protein represents MgtC and the orange protein represents NikR. However, the two histidine residues and the cysteine residue present in NikR that serve as the chelating residues are modified to <scene name='69/698113/Sub_residues_of_chelat/4'>threonine, proline, and isoleucine</scene> respectively. These substitutions likely prevent any chelating activity by MgtC. <ref name="mgtc"/> | ||
[[Image:Combined_overlaps.png |458 x 210 px|thumb|center|'''Figure 1. Overlap of the C-terminal Domain of MgtC with ACT domains of known function.''' 1A shows the significant overlap of the C-terminal of MgtC with SerA, an ACT domain that has been established to bind amino acids. 1B shows the overlap of the C-terminal domain of MgtC with NikR, a known chelating ACT domain.]] | [[Image:Combined_overlaps.png |458 x 210 px|thumb|center|'''Figure 1. Overlap of the C-terminal Domain of MgtC with ACT domains of known function.''' 1A shows the significant overlap of the C-terminal of MgtC with SerA, an ACT domain that has been established to bind amino acids. 1B shows the overlap of the C-terminal domain of MgtC with NikR, a known chelating ACT domain.]] | ||