Figure 2.
FIGURE 2. Secondary structure elements of PhTET1. A,
schematic representation of the PhTET1-12s dimer along the
2-fold symmetry axis, as it appears viewed from the exterior of
the dodecameric complex (see Fig. 3A, left). In each monomer,
catalytic domains are colored in orange and magenta,
dimerization domains in blue, and cobalt ions in green.
Dimerization is achieved through formation of contacts between
the dimerization domain of one monomer and a mixed four-stranded
-sheet (magenta) present
in the catalytic domain of the other monomer. B, multiple
sequence alignment indicating the secondary structure elements
in PhTET1, assigned with DSSP (38), colored as in A. The
abbreviations and GenBank^TM accession numbers of the sequences
are as follows: TET1, P. horikoshii TET1 (AP000002); TET2, P.
horikoshii TET2 (AP000006); YsdC, B. subtilis YsdC protein
(Z75208, Z99118); and AAP, aminopeptidase Ap1 from Vibrio
proteolyticus (M85159, Z11993). The conserved metal-binding
residues are indicated by a ball and the catalytic residues by a
star (according to the MEROPS data base assignment).
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
36327-36337)
copyright 2006.
-sheet (magenta) present
in the catalytic domain of the other monomer. B, multiple
sequence alignment indicating the secondary structure elements
in PhTET1, assigned with DSSP (38), colored as in A. The
abbreviations and GenBank^TM accession numbers of the sequences
are as follows: TET1, P. horikoshii TET1 (AP000002); TET2, P.
horikoshii TET2 (AP000006); YsdC, B. subtilis YsdC protein
(Z75208, Z99118); and AAP, aminopeptidase Ap1 from Vibrio
proteolyticus (M85159, Z11993). The conserved metal-binding
residues are indicated by a ball and the catalytic residues by a
star (according to the MEROPS data base assignment).