A1 Refereed original research article in a scientific journal
Novel calcium recognition constructions in proteins: Calcium blade and EF-hand zone
Authors: Denesyuk AI, Permyakov SE, Johnson MS, Permyakov EA, Denessiouk K
Publisher: ACADEMIC PRESS INC ELSEVIER SCIENCE
Publication year: 2017
Journal: Biochemical and Biophysical Research Communications
Journal name in source: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Journal acronym: BIOCHEM BIOPH RES CO
Volume: 483
Issue: 3
First page : 958
Last page: 963
Number of pages: 6
ISSN: 0006-291X
eISSN: 1090-2104
DOI: https://doi.org/10.1016/j.bbrc.2017.01.040
Abstract
Metal ions can regulate various cell processes being first, second or third messengers, and some of them, especially transition metal ions, take part in catalysis in many enzymes. As an intracellular ion, Ca2+ is involved in many cellular functions from fertilization and contraction, cell differentiation and proliferation, to apoptosis and cancer. Here, we have identified and described two novel calcium recognition environments in proteins: the calcium blade zone and the EF-hand zone, common to 12 and 8 different protein families, respectively. Each of the two environments contains three distinct structural elements: (a) the well-known characteristic Dx[DN]xDG motif; (b) an adjacent structurally identical segment, which binds metal ion in the same way between the calcium blade zone and the EF-hand zone; and (c) the following structurally variable segment, which distinguishes the calcium blade zone from the EF-hand zone. Both zones have sequence insertions between the last residue of the zone and calcium binding residues in positions V or VI. The long insertion often connects the active and the calcium binding sites in proteins. Using the structurally identical segments as an anchor, we were able to construct the classical calmodulin type EF-hand calcium-binding site out of two different calcium binding motifs from two unrelated proteins. (C) 2017 Elsevier Inc. All rights reserved.
Metal ions can regulate various cell processes being first, second or third messengers, and some of them, especially transition metal ions, take part in catalysis in many enzymes. As an intracellular ion, Ca2+ is involved in many cellular functions from fertilization and contraction, cell differentiation and proliferation, to apoptosis and cancer. Here, we have identified and described two novel calcium recognition environments in proteins: the calcium blade zone and the EF-hand zone, common to 12 and 8 different protein families, respectively. Each of the two environments contains three distinct structural elements: (a) the well-known characteristic Dx[DN]xDG motif; (b) an adjacent structurally identical segment, which binds metal ion in the same way between the calcium blade zone and the EF-hand zone; and (c) the following structurally variable segment, which distinguishes the calcium blade zone from the EF-hand zone. Both zones have sequence insertions between the last residue of the zone and calcium binding residues in positions V or VI. The long insertion often connects the active and the calcium binding sites in proteins. Using the structurally identical segments as an anchor, we were able to construct the classical calmodulin type EF-hand calcium-binding site out of two different calcium binding motifs from two unrelated proteins. (C) 2017 Elsevier Inc. All rights reserved.
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