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Updated: Apr 30, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Secondary structure preferences of mn (2+) binding sites in bacterial proteins
Tatyana Aleksandrovna Khrustaleva1
1Regulatory Proteins and Peptides Laboratory, Institute of Physiology of the National Academy of Sciences of Belarus, Akademicheskaya 28, 220072 Minsk, Belarus.
Abstract:
3D structures of proteins with coordinated Mn(2+) ions from bacteria with low, average, and high genomic GC-content have been analyzed (149 PDB files were used). Major Mn(2+) binders are aspartic acid (6.82% of Asp residues), histidine (14.76% of His residues), and glutamic acid (3.51% of Glu residues). We found out that the motif of secondary structure "beta strand-major binder-random coil" is overrepresented around all the three major Mn(2+) binders. That motif may be followed by either alpha helix or beta strand. Beta strands near Mn(2+) binding residues should be stable because they are enriched by such beta formers as valine and isoleucine, as well as by specific combinations of hydrophobic and hydrophilic amino acid residues characteristic to beta sheet. In the group of proteins from GC-rich bacteria glutamic acid residues situated in alpha helices frequently coordinate Mn(2+) ions, probably, because of the decrease of Lys usage under the influence of mutational GC-pressure. On the other hand, the percentage of Mn(2+) sites with at least one amino acid in the "beta strand-major binder-random coil" motif of secondary structure (77.88%) does not depend on genomic GC-content.
Insights
Bacterial protein structures reveal manganese (Mn2+) primarily binds to aspartic acid, histidine, and glutamic acid. A specific secondary structure motif near these binders is common across bacteria, irrespective of their genomic GC-content.
Area of Science:
- Biochemistry
- Structural Biology
- Genomics
Background:
- Genomic GC-content influences bacterial protein structures and functions.
- Manganese (Mn2+) is a crucial cofactor in many bacterial enzymes.
- Understanding Mn2+ coordination in proteins provides insights into metalloenzyme mechanisms.
Purpose of the Study:
- To analyze the 3D structures of bacterial proteins coordinating Mn2+ ions.
- To investigate the relationship between genomic GC-content and Mn2+ binding sites.
- To identify common structural motifs involved in Mn2+ coordination.
Main Methods:
- Analysis of 149 protein data bank (PDB) files of bacterial proteins with Mn2+.
- Identification of major Mn2+ coordinating amino acid residues (Asp, His, Glu).
- Characterization of secondary structure motifs surrounding Mn2+ binding sites.
Main Results:
- Aspartic acid, histidine, and glutamic acid are the primary Mn2+ binders.
- A "beta strand-major binder-random coil" motif is significantly overrepresented around Mn2+ binding sites.
- This motif's prevalence (77.88%) is independent of bacterial genomic GC-content.
- GC-rich bacteria show increased Mn2+ coordination by glutamic acid in alpha helices, potentially due to reduced lysine usage.
Conclusions:
- A conserved secondary structure motif facilitates Mn2+ binding in bacterial proteins.
- Genomic GC-content may influence specific amino acid choices for Mn2+ coordination (e.g., Glu in alpha helices in GC-rich bacteria).
- The identified motif represents a stable and common feature for Mn2+ binding across diverse bacterial genomes.
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