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PDBsum entry 4xq1
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Oxygen binding protein
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PDB id
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4xq1
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References listed in PDB file
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Key reference
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Title
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The bacteriohemerythrin from methylococcus capsulatus (bath): crystal structures reveal that leu114 regulates a water tunnel.
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Authors
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K.H.Chen,
P.Chuankhayan,
H.H.Wu,
C.J.Chen,
M.Fukuda,
S.S.Yu,
S.I.Chan.
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Ref.
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J Inorg Biochem, 2015,
150,
81-89.
[DOI no: ]
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PubMed id
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Abstract
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The bacteriohemerythrin (McHr) from Methylococcus capsulatus (Bath) is an oxygen
carrier that serves as a transporter to deliver O2 from the cytosol of the
bacterial cell body to the particulate methane monooxygenase residing in the
intracytoplasmic membranes for methane oxidation. Here we report X-ray protein
crystal structures of the recombinant wild type (WT) McHr and its L114A, L114Y
and L114F mutants. The structure of the WT reveals a possible water tunnel in
the McHr that might be linked to its faster autoxidation relative to hemerythrin
in marine invertebrates. With Leu114 positioned at the end of this putative
water tunnel, the hydrophobic side chain of this residue seems to play a
prominent role in controlling the access of the water molecule required for
autoxidation. This hypothesis is examined by comparing the autoxidation rates of
the WT McHr with those of the L114A, L114Y and L114F mutants. The biochemical
data are correlated with structural insights derived from the analysis of the
putative water tunnels in the various McHr proteins provided by the X-ray
structures.
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