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PDBsum entry 1a7d
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Oxygen transport
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PDB id
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1a7d
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Contents |
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* Residue conservation analysis
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DOI no:
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Biochemistry
36:7044-7049
(1997)
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PubMed id:
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Structures of wild-type chloromet and L103N hydroxomet Themiste zostericola myohemerythrins at 1.8 A resolution.
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L.J.Martins,
C.P.Hill,
W.R.Ellis.
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ABSTRACT
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Myohemerythrin (Mhr) is a nonheme iron oxygen carrier found in the retractor
muscles of marine "peanut" worms. The X-ray crystal structures of two
recombinant Themiste zostericola Mhrs are reported to a resolution of 1.8 A.
Surprisingly, the met wild-type structure (R = 17.8%) was found to contain
chloride bound to Fe2, while coordinated hydroxide was found in the met L103N
structure (R = 18.3%). An internal water molecule was also found distal to the
Fe-O-Fe center of the mutant protein, forming hydrogen bonds with the
coordinated hydroxide and the OD1 atom of Asn-103. This finding is consistent
with the kinetic and spectroscopic results reported for the L103N mutant Mhr
[Raner, G. M., Martins, L. J., & Ellis, W. R., Jr. (1997) Biochemistry 36,
7037-7043]. Possible roles for the side chain of residue 103 (Leu in wild-type
Mhr) in gating ligand binding are also discussed.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.A.Larrabee,
W.R.Johnson,
and
A.S.Volwiler
(2009).
Magnetic circular dichroism study of a dicobalt(II) complex with mixed 5- and 6-coordination: a spectroscopic model for dicobalt(II) hydrolases.
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Inorg Chem,
48,
8822-8829.
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O.A.Karlsen,
L.Ramsevik,
L.J.Bruseth,
Ã.˜.Larsen,
A.Brenner,
F.S.Berven,
H.B.Jensen,
and
J.R.Lillehaug
(2005).
Characterization of a prokaryotic haemerythrin from the methanotrophic bacterium Methylococcus capsulatus (Bath).
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FEBS J,
272,
2428-2440.
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V.Adam,
A.Royant,
V.Nivière,
F.P.Molina-Heredia,
and
D.Bourgeois
(2004).
Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction.
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Structure,
12,
1729-1740.
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PDB codes:
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M.Merkx,
D.A.Kopp,
M.H.Sazinsky,
J.L.Blazyk,
J.Müller,
and
S.J.Lippard
(2001).
Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins A list of abbreviations can be found in Section 7.
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Angew Chem Int Ed Engl,
40,
2782-2807.
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J.Xiong,
R.S.Phillips,
D.M.Kurtz,
S.Jin,
J.Ai,
and
J.Sanders-Loehr
(2000).
The O(2) binding pocket of myohemerythrin: role of a conserved leucine.
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Biochemistry,
39,
8526-8536.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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