TY - JOUR
T1 - New perspectives of zinc coordination environments in proteins
AU - Maret, Wolfgang
N1 - Copyright © 2011 Elsevier Inc. All rights reserved.
PY - 2012/6
Y1 - 2012/6
N2 - Zinc is more widely used as a cofactor in proteins than any other transition metal ion. In addition to catalytic and structural functions, zinc(II) ions have a role in information transfer and cellular control. They bind transiently when proteins regulate zinc concentrations and re-distribute zinc and when proteins are regulated by zinc. Transient zinc-binding sites employ the same donors of amino acid side chains as catalytic and structural sites but differ in their coordination chemistry that can modulate zinc affinities over at least ten orders of magnitude. Redox activity of the cysteine ligands, multiple binding modes of the oxygen, sulfur and nitrogen donors, and protein conformational changes induce coordination dynamics in zinc sites and zinc ion mobility. Functional annotations of the remarkable variation of coordination environments in zinc proteomes need to consider how the primary coordination spheres interact with protein structure and dynamics, and the adaptation of coordination properties to the biological context in extracellular, cellular, or subcellular locations.
AB - Zinc is more widely used as a cofactor in proteins than any other transition metal ion. In addition to catalytic and structural functions, zinc(II) ions have a role in information transfer and cellular control. They bind transiently when proteins regulate zinc concentrations and re-distribute zinc and when proteins are regulated by zinc. Transient zinc-binding sites employ the same donors of amino acid side chains as catalytic and structural sites but differ in their coordination chemistry that can modulate zinc affinities over at least ten orders of magnitude. Redox activity of the cysteine ligands, multiple binding modes of the oxygen, sulfur and nitrogen donors, and protein conformational changes induce coordination dynamics in zinc sites and zinc ion mobility. Functional annotations of the remarkable variation of coordination environments in zinc proteomes need to consider how the primary coordination spheres interact with protein structure and dynamics, and the adaptation of coordination properties to the biological context in extracellular, cellular, or subcellular locations.
U2 - 10.1016/j.jinorgbio.2011.11.018
DO - 10.1016/j.jinorgbio.2011.11.018
M3 - Article
C2 - 22196021
VL - 111
SP - 110
EP - 116
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
ER -