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Results: 6

1.

Figure. From: The rhodanese/Cdc25 phosphatase superfamily.

Domenico Bordo, et al. EMBO Rep. 2002 August 15;3(8):741-746.
2.

Figure. From: The rhodanese/Cdc25 phosphatase superfamily.

Domenico Bordo & Peer Bork

Domenico Bordo, et al. EMBO Rep. 2002 August 15;3(8):741-746.
3.

Figure. From: The rhodanese/Cdc25 phosphatase superfamily.

Fig. 1. Scheme representing the sulfur-transfer reaction catalyzed by rhodanese.

Domenico Bordo, et al. EMBO Rep. 2002 August 15;3(8):741-746.
4.

Figure. From: The rhodanese/Cdc25 phosphatase superfamily.

Fig. 4. Co-occurrence of rhodanese modules in association with other protein domains. Domains are schematized as colored boxes. Catalytic rhodanese modules with a six-amino-acid active-site loop are shown in red, and inactive rhodanese modules are displayed in black. Rhodanese modules with a seven-amino-acid active-site loop are displayed in yellow. Other protein domains are shown in gray. Active-site loop positions displaying at least 80% amino-acids conservation within each subfamily are also shown as conserved motifs.

Domenico Bordo, et al. EMBO Rep. 2002 August 15;3(8):741-746.
5.

Figure. From: The rhodanese/Cdc25 phosphatase superfamily.

Fig. 2. Three-dimensional structure of A. vinelandii RhdA and of human Cdc25A phosphatase, superimposed on their respective catalytic domains. RhdA and Cdc25A are shown in blue and yellow, respectively. Active-site loops and the structurally equivalent loop on the RhdA N-terminal domain are shown in red. The catalytic Cys and the Asp counterpart on the inactive domain are represented in ball-and-stick. Conserved residues, Tyr37 and His41 (RhdA numbering), putatively involved in regulative function (see text) are also shown. The linker polypeptide connecting the two RhdA domains is shown in pink. The βC–αC loops involved in RhdA in interdomain interaction (Bordo et al., 2000) are shown in green.

Domenico Bordo, et al. EMBO Rep. 2002 August 15;3(8):741-746.
6.

Figure. From: The rhodanese/Cdc25 phosphatase superfamily.

Fig. 3. Neighbor-joining tree representing the rhodanese superfamily generated by CLUSTALW (correction for multiple substitution was adopted; Thompson et al., 1997). The multiple alignment was derived from that included in the SMART resource, to which four E. coli, two archaea and two ThiI proteins were added, for a total of 155 rhodanese modules. The SMART alignment represents an even sample of the total number of rhodanese modules, as closely related sequences are represented only once. The tree was displayed and validated by bootstrap analysis using programs in the PHYLIP package (Felsenstein, 1989). Archaeal, bacterial and eukaryotic proteins are represented in blue, red and green, respectively. Symbols are used to indicate the distinct structural or functional roles of the rhodanese modules, as described in the inset.

Domenico Bordo, et al. EMBO Rep. 2002 August 15;3(8):741-746.

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