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Figure 3.
Structure of the catalytic domain of SENP7. A, two views of
the SENP7 catalytic domain shown in ribbon representation.
Secondary structure elements are either numbered (β-strands) or
lettered (α-helices). The catalytic residues are depicted in
stick representation near the top of each panel, and the
catalytic cysteine is labeled (C926). The insertion elements
(Loop-1, Loop-2, Loop-3, and Loop-4) are labeled in at least one
of the two panels. Segments of the polypeptide not observed in
the electron density maps were deemed disordered and are
indicated by dashed lines. The N and C termini are labeled N or
C, respectively. B, superposition of the SENP7 and SENP2 (PDB
1THO) structures in ribbon representation with SENP7 colored
blue and SENP2 colored yellow. Catalytic residues are shown in
stick representation as in A. C, superposition of SENP1 (PDB
2IYC) with SENP2 (PDB 1THO) in ribbon representation with SENP1
colored green and SENP2 colored yellow. Catalytic residues are
shown in stick representation. D, alignment of sequences
corresponding to the catalytic domains for human SENP7, SENP6,
SENP1, SENP2, and SENP3 based on structural alignment of human
SENP2 and SENP7. Gaps are denoted by dots and the large sequence
insertion within Loop-3 is depicted by // to indicate that the
sequence is missing from the alignment. Numbering above the
sequence alignment corresponds to the amino acid position in
full-length SENP7. Secondary structural elements are indicated
above the alignment for SENP7 (blue) and below the alignment for
SENP2 (yellow). For SENP7, β-strands are numbered, α-helices
lettered, and coil depicted as a line. Missing regions in our
structure are denoted by dashed lines, and the gap in Loop-3 is
indicated by //. Side chain identity (75% conservation) is
denoted in the alignment by a yellow background. Conserved
catalytic residues are depicted in red. Graphics were prepared
with PYMOL (47).
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