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PDBsum entry 1jf3
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Oxygen storage/transport
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PDB id
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1jf3
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structures of unligated and cn-Ligated glycera dibranchiata monomer ferric hemoglobin components III and IV.
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Authors
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H.J.Park,
C.Yang,
N.Treff,
J.D.Satterlee,
C.Kang.
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Ref.
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Proteins, 2002,
49,
49-60.
[DOI no: ]
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PubMed id
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Abstract
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Erythrocytes of the marine annelid, Glycera dibranchiata, contain a mixture of
monomeric and polymeric hemoglobins. There are three major monomer hemoglobin
components, II, III, IV (also called GMH2, 3, and 4), that have been highly
purified and well characterized. We have now crystallized GMH3 and GMH4 and
determined their structures to 1.4-1.8 A resolution. The structures were
determined for these two monomer hemoglobins in the oxidized (Fe3+, ferric, or
met-) forms in both the unligated and cyanide-ligated states. This work differs
from two published, refined structures of a Glycera dibranchiata monomer
hemoglobin, which has a sequence that is substantially different from any bona
fide major monomer hemoglobins (GMH2, 3, or 4). The high-resolution crystal
structures (presented here) and the previous NMR structure of CO-ligated GMH4,
provide a basis for interpreting structure/function details of the monomer
hemoglobins. These details include: (1) the strong correlation between
temperature factor and NMR dynamics for respective protein forms; (2) the unique
nature of the HisE7Leu primary sequence substitutions in GMH3 and GMH4 and their
impact on cyanide ion binding kinetics; (3) the LeuB10Phe difference between
GMH3 and GMH4 and its impact on ligand binding; and (4) elucidation of changes
in the structural details of the distal and proximal heme pockets upon cyanide
binding.
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Figure 4.
Figure 4. Illustration of heme-b, the prosthetic group of the
G. dibranchiata monomer hemoglobins, labeled according to the
crystallographic convention. Fischer numberings of the pyrrole
carbons are shown in parentheses.
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Figure 8.
Figure 8. Superimposed views of heme and selected heme pocket
amino acid residues of: (A) GMH3: unligated (red) and CN-ligated
(green); and (B) GMH4: unligated (blue) and CN-ligated
(yellow-green).
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2002,
49,
49-60)
copyright 2002.
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