1uku
From Proteopedia
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Crystal Structure of Pyrococcus horikoshii CutA1 Complexed with Cu2+
Overview
CutA is a small protein that appears to be involved in the mechanism of, divalent metal cation tolerance in microorganisms. Here we report the, crystal structure of Pyrococcus horikoshii CutA (PhoCutA), with and, without Cu(2+), and its metal-binding properties. Crystallographic, analyses revealed that PhoCutA forms a stable trimeric structure with, intertwined antiparallel beta-strands. The crystal structure of the, Cu(2+)-PhoCutA complex shows that the Cu(2+) is located at a trimer-trimer, interface and is recognized by the side chains of one Asp(48) from each, trimer. In an in vitro experiment, PhoCutA bound to several heavy metals, most of which led to reversible aggregation of the protein; i.e. the, aggregates could be completely solubilized by addition of ethylenediamine, tetraacetic acid (EDTA) or dialysis against metal free buffer., Substitution of Asp(48) with Ala led to a decrease in the amount of, aggregates, suggesting the significant contribution of Asp(48) to the, reversible aggregation. To the best of our knowledge, this is the first, report which provides the structural evidence for heavy metal-induced, multimerization of a protein.
About this Structure
1UKU is a Single protein structure of sequence from Pyrococcus horikoshii with CU as ligand. Full crystallographic information is available from OCA.
Reference
Structural implications for heavy metal-induced reversible assembly and aggregation of a protein: the case of Pyrococcus horikoshii CutA., Tanaka Y, Tsumoto K, Nakanishi T, Yasutake Y, Sakai N, Yao M, Tanaka I, Kumagai I, FEBS Lett. 2004 Jan 2;556(1-3):167-74. PMID:14706845
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