PDBsum entry 1j2v

Structural genomics, unknown function

PDB id: 1j2v

Contents

Protein chain

102 a.a. *

Waters ×36

* Residue conservation analysis

PDB id:

1j2v

Name:

Structural genomics, unknown function

Title:

Crystal structure of cuta1 from pyrococcus horikoshii

Structure:

102aa long hypothetical periplasmic divalent cation tolerance protein cuta. Chain: a. Synonym: cuta1, cuta1 homology protein ph0992. Engineered: yes. Mutation: yes

Source:

Pyrococcus horikoshii. Organism_taxid: 70601. Strain: ot3. Gene: ph0992. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Trimer (from PDB file)

Resolution:

2.00Å R-factor: 0.239 R-free: 0.287

Authors:

Y.Tanaka,N.Sakai,Y.Yasutake,M.Yao,K.Tsumoto,I.Kumagai,I.Tanaka

Key ref:

Y.Tanaka et al. (2004). Structural implications for heavy metal-induced reversible assembly and aggregation of a protein: the case of Pyrococcus horikoshii CutA. FEBS Lett, 556, 167-174. PubMed id: 14706845 DOI: 10.1016/S0014-5793(03)01402-9

Date:

11-Jan-03 Release date: 13-Jan-04

Protein chain

O58720  (CUTA_PYRHO) -  Divalent-cation tolerance protein CutA from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

Seq: 102 a.a.

Struc: 102 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1016/S0014-5793(03)01402-9

FEBS Lett 556:167-174 (2004)

PubMed id: 14706845

Structural implications for heavy metal-induced reversible assembly and aggregation of a protein: the case of Pyrococcus horikoshii CutA.

Y.Tanaka, K.Tsumoto, T.Nakanishi, Y.Yasutake, N.Sakai, M.Yao, I.Tanaka, I.Kumagai.

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.

Selected figure(s)

Figure 3.
Fig. 3. Structure of PhoCutA complexed with copper. A: Superposition of the Cα trace of PhoCutA without Cu^2+ (blue) and complexed with Cu^2+ (red). Cu^2+ (green ball) and Asp^48 (ball-and-stick) are also shown. B: Ribbon diagram of dimer of trimeric structures. Copper ion (Cu^2+) is shown as a green ball in the trimer–trimer interface. C: Deduced structure of multimer induced by Cu^2+ binding. Cu^2+ is green, proteins in the first layer are blue, and proteins in the second layer are red. D: Cu^2+-binding site of PhoCutA. Each trimer is colored blue or red. Cu^2+-binding residues (ball-and-stick representations) and water molecules (red balls) are shown.

Figure 4.
Fig. 4. SDS–PAGE of PhoCutA untreated by metals.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2004, 556, 167-174) copyright 2004.

Figures were selected by an automated process.