Gi. Birnbaum et al., 1.70 ANGSTROM RESOLUTION STRUCTURE OF MYOGLOBIN FROM YELLOWFIN TUNA -AN EXAMPLE OF A MYOGLOBIN LACKING THE D-HELIX, Acta crystallographica. Section D, Biological crystallography, 50, 1994, pp. 283-289
The crystal structure of metmyoglobin from yellowfin tuna (Thunnus alb
acares) has been determined by molecular replacement methods and refin
ed to a conventional R factor of 0.177 for all observed reflections in
the range of 6.0-1.70 angstrom resolution. Like other myoglobins for
which a high-resolution structure is available, the polypeptide chain
is organized into several helices that cooperate to form a hydrophobic
pocket into which the heme prosthetic group is non-covalently bound;
however, the D helix observed in other myoglobins is absent in myoglob
in from yellowfin tuna and has been replaced with a random coil. As we
ll, the A helix has a pronounced kink due to the presence of Pro16. Th
e differences in structure between this and sperm whale myoglobin can
be correlated with their reported dioxygen affinity and dissociation.
The structure is in agreement with reported fluorescence data which sh
ow an increased Trp14...heme distance in yellowfin tuna compared to sp
erm whale myoglobin.