1uku
From Proteopedia
(New page: 200px<br /><applet load="1uku" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uku, resolution 1.45Å" /> '''Crystal Structure of...) |
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| - | [[Image:1uku.jpg|left|200px]]<br /><applet load="1uku" size=" | + | [[Image:1uku.jpg|left|200px]]<br /><applet load="1uku" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uku, resolution 1.45Å" /> | caption="1uku, resolution 1.45Å" /> | ||
'''Crystal Structure of Pyrococcus horikoshii CutA1 Complexed with Cu2+'''<br /> | '''Crystal Structure of Pyrococcus horikoshii CutA1 Complexed with Cu2+'''<br /> | ||
==Overview== | ==Overview== | ||
| - | CutA is a small protein that appears to be involved in the mechanism of | + | 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== | ==About this Structure== | ||
| - | 1UKU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1UKU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UKU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:37 2008'' |
Revision as of 13:25, 21 February 2008
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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 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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