Literature DB >> 21315656

Bacterial protein structures reveal phylum dependent divergence.

Matthew D Shortridge1, Thomas Triplet, Peter Revesz, Mark A Griep, Robert Powers.   

Abstract

Protein sequence space is vast compared to protein fold space. This raises important questions about how structures adapt to evolutionary changes in protein sequences. A growing trend is to regard protein fold space as a continuum rather than a series of discrete structures. From this perspective, homologous protein structures within the same functional classification should reveal a constant rate of structural drift relative to sequence changes. The clusters of orthologous groups (COG) classification system was used to annotate homologous bacterial protein structures in the Protein Data Bank (PDB). The structures and sequences of proteins within each COG were compared against each other to establish their relatedness. As expected, the analysis demonstrates a sharp structural divergence between the bacterial phyla Firmicutes and Proteobacteria. Additionally, each COG had a distinct sequence/structure relationship, indicating that different evolutionary pressures affect the degree of structural divergence. However, our analysis also shows the relative drift rate between sequence identity and structure divergence remains constant.
Copyright © 2011 Elsevier Ltd. All rights reserved.

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Year:  2011        PMID: 21315656      PMCID: PMC3049983          DOI: 10.1016/j.compbiolchem.2010.12.004

Source DB:  PubMed          Journal:  Comput Biol Chem        ISSN: 1476-9271            Impact factor:   2.877


  64 in total

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Authors:  Chuong B Do; Kazutaka Katoh
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7.  Tissue-specific expression and promoter analysis of the tobacco Itp1 gene.

Authors:  S Canevascini; D Caderas; T Mandel; A J Fleming; I Dupuis; C Kuhlemeier
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9.  The COG database: an updated version includes eukaryotes.

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10.  Annotation error in public databases: misannotation of molecular function in enzyme superfamilies.

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Journal:  PLoS Comput Biol       Date:  2009-12-11       Impact factor: 4.475

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  2 in total

1.  ¹H, ¹³C, and ¹⁵N NMR assignments for the helicase interaction domain of Staphylococcus aureus DnaG primase.

Authors:  Matthew D Shortridge; Mark A Griep; Robert Powers
Journal:  Biomol NMR Assign       Date:  2011-06-07       Impact factor: 0.746

2.  Identification of a Ligand-Binding Site on the Staphylococcus aureus DnaG Primase C-Terminal Domain.

Authors:  Jonathan Catazaro; Jessica Periago; Matthew D Shortridge; Bradley Worley; Andrew Kirchner; Robert Powers; Mark A Griep
Journal:  Biochemistry       Date:  2017-02-09       Impact factor: 3.162

  2 in total

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