To commemorate this occasion and the sucessful scientific career
preceeding it, a sculpture of aminoimidazole ribonucleotide (AIR) was
commissioned and presented by Dr. Erik
Meyer. In 1999, A new intermediate and two new enzymatic
activities in the
purine biosynthetic pathway in prokaryotes were reported(1).
Atomic coordinates(2) from
the X-ray
crystal structure (1D7A.PDB) were used to create a scaled molecular
model.
An appropriate slab (20 x 30 x 8 cm3)
of seasoned oak was selected
and
mounted for milling.
The atomic coordinates of the substrate
adduct found in
the Protein Data Bank (1D7A.PDB) together with orientation and setup
parameters
appropriate for he slab were input to program SCULPT, which provided "G
code"
for a CNC milling machine in the Molecular Sculptures shop at Taos, NM (3).
Both faces of the slab were milled in a
2-step
process,
first removing wood above the
atomic surfaces in a lateral motion (G01),
followed by rotational carving of descending planes (G03) to reveal the
three-dimensional surface of the molecular model.
In order to obtain
a
three-dimensional model, the partially carved model was first
stabilized in
preparation for the loss of lateral support and the slab was flipped prior to
carving the
reverse side. The lateral forces of the CNC milling machine are
considerable
and the emerging sculpture would become unstable if not supported. In
carving
the reverse side, it is essential
that the structural origin and axis of rotation remain unchanged; this
was
satisfactorily obtained.
A citation and
reference was
inscribed.
After light
sanding, the
sculpture was finished with multiple coats of polyurethane spar
varnish.
The
cutting tool path is depicted:
_ _ _
(1) Evidence for the Direct Transfer
of the Carboxylate of N5-Carboxyaminoimidazole Ribonucleotide (N5-CAIR)
To Generate 4-Carboxy-5-aminoimidazole
Ribonucleotide Catalyzed by
Escherichia coli PurE, an
N5-CAIR Mutase;
Erik Meyer, T. Joseph Kappock, Chukwunenye Osuji, and JoAnne
Stubbe; Biochemistry (1999), 38,
3012-3018
(2)
Crystal structure of Escherichia coli
PurE, an unusual mutase in the purine biosynthetic pathway
I.I.Mathews,T.J.Kappock,J.Stubbe,S.E.Ealick; Structure
(1999) 7: 1395
(3) Supported in part by a grant
from the U.S. National Science Foundation through the University of New
Mexico - Taos.
