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PDBsum entry 1myt
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Oxygen transport
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PDB id
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1myt
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References listed in PDB file
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Key reference
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Title
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1.70 a resolution structure of myoglobin from yellowfin tuna. An example of a myoglobin lacking the d helix.
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Authors
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G.I.Birnbaum,
S.V.Evans,
M.Przybylska,
D.R.Rose.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1994,
50,
283-289.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of metmyoglobin from yellowfin tuna (Thunnus albacares)
has been determined by molecular replacement methods and refined to a
conventional R factor of 0.177 for all observed reflections in the range of
6.0-1.70 A 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 myoglobin from yellowfin tuna and has been replaced with a random
coil. As well, the A helix has a pronounced kink due to the presence of Pro16.
The 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 show an increased
Trp14.heme distance in yellowfin tuna compared to sperm whale myoglobin.
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Figure 4.
Fig. 4. Aignment of the primary
sequence of YFT and SW myo-
glbin.
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Figure 8.
Fig. 8. Stereoview of the heme group and its distal an proximal histidine groups, and their corresponding electron dnsity. The heme
iron is diplaed by 0.09 A out of the mean plane of the pyrrole N atoms toward the heme ligand His93.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1994,
50,
283-289)
copyright 1994.
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Secondary reference #1
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Title
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Structure of yellow fin tuna metmyoglobin at 6 angstroms resolution
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Authors
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E.E.Lattman,
C.E.Nockolds,
R.H.Kretsinger,
W.E.Love.
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Ref.
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j mol biol, 1971,
60,
271.
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