2016
DOI: 10.1016/j.jtbi.2016.02.006
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Magnesium and manganese binding sites on proteins have the same predominant motif of secondary structure

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Cited by 31 publications
(16 citation statements)
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“…Therefore, the Mg(II) can interfere with the detection of Pd(II). To the best of our knowledge, amino acid residues alone [25] or hydrophilic amino acids such as asparagine and glutamine at certain positions in a peptide can provide an ideal environment to coordinate Mg(II), similar to the complex reported in the previous report [26]. Therefore, the colorimetric method detecting Pd(II) is certainly applicable to the specific circumstances of wastewater produced from Pdcatalyzed organic reactions and glassware contaminated with Pd(II).…”
Section: Selectivitysupporting
confidence: 58%
“…Therefore, the Mg(II) can interfere with the detection of Pd(II). To the best of our knowledge, amino acid residues alone [25] or hydrophilic amino acids such as asparagine and glutamine at certain positions in a peptide can provide an ideal environment to coordinate Mg(II), similar to the complex reported in the previous report [26]. Therefore, the colorimetric method detecting Pd(II) is certainly applicable to the specific circumstances of wastewater produced from Pdcatalyzed organic reactions and glassware contaminated with Pd(II).…”
Section: Selectivitysupporting
confidence: 58%
“…Thus, generally few differences exist between Mg and Mn coordination spheres responsible for the cation specificity. Khrustalev et al [27] investigated several hundred Mn and Mg metalloproteins and found that Mg and Mn are typically bound to oxygen in the carboxylate groups of Asp and Glu. Histidine (His) residues appear underrepresented in Asp and Glu rich pockets binding Mg 2+ , while His groups are overrepresented in Asp and Glu pockets binding Mn 2+ .…”
Section: Manganese In Metalloenzymesmentioning
confidence: 99%
“…We chose the 197 residue‐AAV5 Rep nuclease domain in complex with Mg 2+ (PDB Code: 1UUT; hereafter referred to as AAV5 Rep197) as our model for further studies because 1) all the bioinformatics tools used predicted SIRV1 Rep metal‐binding with this complex as a model; 2) the metal‐coordinating residues are identical, and 3) the superimposed active site residues of both model and query have the minimum root mean square deviation (RMSD) of all active sites compared, and therefore represented the best match. Although the model used comprised of Mg 2+ , structural studies have indicated that both Mg 2+ and Mn 2+ use identical coordination chemistries .…”
Section: Resultsmentioning
confidence: 99%