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PDBsum entry 2lp3
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Metal binding protein
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PDB id
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2lp3
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References listed in PDB file
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Key reference
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Title
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Impact of calcium binding and thionylation of s100a1 protein on its nuclear magnetic resonance-Derived structure and backbone dynamics.
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Authors
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M.Nowakowski,
K.Ruszczyńska-Bartnik,
M.Budzińska,
L.Jaremko,
M.Jaremko,
K.Zdanowski,
A.Bierzyński,
A.Ejchart.
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Ref.
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Biochemistry, 2013,
52,
1149-1159.
[DOI no: ]
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PubMed id
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Abstract
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S100 proteins play a crucial role in multiple important biological processes in
vertebrate organisms acting predominantly as calcium signal transmitters. S100A1
is a typical representative of this family of proteins. After four Ca(2+) ions
bind, it undergoes a dramatic conformational change, resulting in exposure, in
each of its two identical subunits, a large hydrophobic cleft that binds to
target proteins. It has been shown that abnormal expression of S100A1 is
strongly correlated with a number of severe human diseases: cardiomyopathy and
neurodegenerative disorders. A few years ago, we found that thionylation of Cys
85, the unique cysteine in two identical S100A1 subunits, leads to a drastic
increase of the affinity of the protein for calcium. We postulated that the
protein activated by thionylation becomes a more efficient calcium signal
transmitter. Therefore, we decided to undertake, using nuclear magnetic
resonance methods, a comparative study of the structure and dynamics of native
and thionylated human S100A1 in its apo and holo states. In this paper, we
present the results obtained for both forms of this protein in its holo state
and compare them with the previously published structure of native apo-S100. The
main conclusion that we draw from these results is that the increased calcium
binding affinity of S100A1 upon thionylation arises, most probably, from
rearrangement of the hydrophobic core in its apo form.
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