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| {{STRUCTURE_1j2v| PDB=1j2v | SCENE= }} | | {{STRUCTURE_1j2v| PDB=1j2v | SCENE= }} |
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| '''Crystal Structure of CutA1 from Pyrococcus Horikoshii'''
| | ===Crystal Structure of CutA1 from Pyrococcus Horikoshii=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14706845}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14706845 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14706845}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Alpha + beta]] | | [[Category: Alpha + beta]] |
| [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:44:11 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:25:10 2008'' |
