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PDBsum entry 1hlm
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Oxygen transport
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PDB id
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1hlm
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References listed in PDB file
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Key reference
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Title
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Amino acid sequence of a globin from the sea cucumber caudina (molpadia) arenicola.
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Authors
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F.Mauri,
J.Omnaas,
L.Davidson,
C.Whitfill,
G.B.Kitto.
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Ref.
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Biochim Biophys Acta, 1991,
1078,
63-67.
[DOI no: ]
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PubMed id
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Abstract
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Coelomic cells from the sea cucumber Caudina (Molpadia) arenicola contain four
major globins, A, B, C and D. The hemoglobins from this organism show unusual
ligand-linked dissociation properties. The complete amino acid sequence of the D
globin has been established. It is N-acetylated, consists of 158 residues and
has a 10 amino acid N-terminal extension similar to that found in some other
invertebrate globins. The C. arenicola D globin has an equal sequence identity
(28%) with both alpha and beta human globins and as anticipated, is more closely
related to these vertebrate proteins than are molluscan globins. The C.
arenicola D globin shows a 59% identity with the globin I from the sea cucumber
Paracaudina chilensis. The availability of the C. arenicola D globin sequence
will aid the X-ray analysis of this protein and facilitate an understanding of
the changes in subunit interactions that occur with cooperative ligand binding.
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Added reference #1*
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Title
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X-ray structure determination of a dimeric hemoglobin from Caudina arenicola.
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Authors
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D.T.Mitchell,
S.R.Ernst,
M.L.Hackert.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1995,
51,
760-766.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. Cot representation of the
concatenated Hb model
(MOLSCRIPT; Kraulis, 1991).
Urechis Hb (yellow), human /~
Hb (green), Scapharca Hb (cyan),
and HbC (black). The major areas
of difference are the N and C
terminii, A/B turn (1), CD loop
region (2), E/F turn (3), and G/H
turn (4). The HbD model is also
superimposed and in red.
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Figure 7.
Fig. 7. Ball-and-stick model of he
Hb-D dimer interface
(MOLSCRIPT; Kraulis, 1991) with
the E helices in green, F helices in
light blue, and heme groups in
purple. Note the large number of
hydrophobic residues as well as
electrostatic interactions along he
interface.
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The above figures are
reproduced from the cited reference
with permission from the IUCr
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*Note, "added" references are those not in the PDB file but
which have either been obtained from the journal or suggested by the
author(s).
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Secondary reference #1
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Title
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Preliminary crystallographic data on monomeric and dimeric hemoglobins from the sea cucumber, Molpadia arenicola.
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Authors
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W.M.Carson,
T.R.Bowers,
G.B.Kitto,
M.L.Hackert.
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Ref.
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J Biol Chem, 1979,
254,
7400-7402.
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PubMed id
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Secondary reference #2
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Title
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N-Terminal substitution of some sea cucumber hemoglobins.
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Authors
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G.B.Kitto,
D.Erwin,
R.West,
J.Omnaas.
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Ref.
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Comp Biochem Physiol B, 1976,
55,
105-107.
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PubMed id
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