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Inventi Impact - Bioinformatics

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  • Inventi:ebi/8835/14
    SECONDARY STRUCTURE PREFERENCES OF MN2+ BINDING SITES IN BACTERIAL PROTEINS
    Tatyana Aleksandrovna Khrustaleva

    3D structures of proteins with coordinated Mn2+ ions from bacteria with low, average, and high genomic GC-content have been analyzed (149 PDB files were used).MajorMn2+ binders are aspartic acid (6.82% ofAsp residues), histidine (14.76% ofHis 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 Mn2+ binders. That motif may be followed by either alpha helix or beta strand. Beta strands nearMn2+ 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 coordinateMn2+ ions, probably, because of the decrease of Lys usage under the influence of mutational GC-pressure. On the other hand, the percentage of Mn2+ 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.

    How to Cite this Article
    CC Compliant Citation: Tatyana Aleksandrovna Khrustaleva, “Secondary Structure Preferences of Mn2+ Binding Sites in Bacterial Proteins,” Advances in Bioinformatics, vol. 2014, Article ID 501841, 14 pages, 2014. doi:10.1155/2014/501841. Copyright © 2014 Tatyana Aleksandrovna Khrustaleva. This is an open access article distributed under the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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