 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](dz5145fig1mag.jpg)
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Figure 1
(a) Sequence alignment of the SRP14 proteins of Arabidopsis thaliana, Caenorhabditis elegans, Canis familiaris, Homo sapiens, Mus musculus, Saccharomyces cerevisiae and Schizosaccharomyces pombe. SRP14 sequences were aligned with ClustalX (Thompson et al., 1997  ) and formatted with ALSCRIPT (Barton, 1993). Aligned residues are highlighted according to the conservation scores of Zvelebil et al. (1987) according to these criteria: positions with a score of >4, light green; score of >5, mid-green; strictly conserved residues, dark green with white lettering. Sequences are numbered according to S. pombe SRP14. Cysteine residues are shown in yellow and such residues of S. pombe Srp14 are boxed. Also boxed is the sequence which has been shown to be essential for elongation arrest (Thomas et al., 1997; Mason et al., 2000; Lakkaraju et al., 2008), which is labelled `Elongation arrest'. The structure presented here is disordered in this region; the carboxy-terminal residues which are ordered are labelled `COOH' for chain A and chain B. Amino acids which are likely to interact with Alu-domain RNA are highlighted with grey asterisks. (b) Schematic diagrams of SRPs from human and S. pombe. The Alu and S domains are labelled. Of particular note are the differences between the two particles in terms of the subunit compositions of the Alu domains. While human SRPs have a pseudo-symmetrical SRP9/14 complex, S. pombe, like other fungi, is believed to possess a homodimer of SRP14 subunits, as shown in Model 1. Model 2 depicts the possible subunit composition of SRP proposed by Rosenblad et al. (2004), in which SRP14 heterodimerizes with SRP21. See text for further discussion. |
![[Figure 1]](dz5145fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
