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Figure 2.
Figure 2. (a) Multiple superimposition of Sm-like protein
structures produced from the MUSTANG program.[15] While the core
 -sheet
structure of these Sm-like proteins superimposed very well, the
 -helices
and loops 4 vary to a great extent. XC5858 (shown in red)
contains an extra N-terminal structure that interacts
substantially with the extended 2
 /
3
structure. (b) Multiple sequence alignments of XC5848 with the
two bacterial Sm-like Hfq proteins (1HK9/1KQ1), the six archaeal
Sm-like proteins (1H64, 1I4K, 1I81, 1I8F, 1LJ0, 1M8V), the two
human Sm-like proteins (1B34, DD3B), and the yeast Sm-like
protein (1N9S) produced from same program. Colors indicate the
chemical nature of the amino acid (small hydrophobic including
aromatic, red; acidic, blue; basic, magenta; basic amino acids
with hydroxyl group and/or amino groups, black). The secondary
structure elements for -helix
(green tube) and -strand
(red arrows) were also shown for the top and bottom sequences,
along with their annotations. The -helices
and -strands
for each individual sequence were boxed in green and red,
respectively. The essential residues responsible for subunit
interactions and/or protein-RNA interactions were further marked
with unique symbols in blue.
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