1J2V

Crystal Structure of CutA1 from Pyrococcus Horikoshii

Summary for 1J2V

• Entry DOI: 10.2210/pdb1j2v/pdb
• Descriptor: 102AA long hypothetical periplasmic divalent cation tolerance protein CUTA (2 entities in total)
• Functional Keywords: alpha + beta, structural genomics, unknown function
• Biological source: Pyrococcus horikoshii
• Cellular location: Cytoplasm: O58720
• Total number of polymer chains: 1
• Total formula weight: 12479.02

Authors

Tanaka, Y.,Sakai, N.,Yasutake, Y.,Yao, M.,Tsumoto, K.,Kumagai, I.,Tanaka, I. (deposition date: 2003-01-11, release date: 2004-01-13, Last modification date: 2024-10-30)

Primary citation

Tanaka, Y.,Tsumoto, K.,Nakanishi, T.,Yasutake, Y.,Sakai, N.,Yao, M.,Tanaka, I.,Kumagai, I.
Structural implications for heavy metal-induced reversible assembly and aggregation of a protein: the case of Pyrococcus horikoshii CutA.
Febs Lett., 556:167-174, 2004

PubMed Abstract: 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.

PubMed: 14706845
DOI: 10.1016/S0014-5793(03)01402-9

Experimental method

X-RAY DIFFRACTION (2 Å)