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PDBsum entry 3eee
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Signaling protein
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PDB id
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3eee
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References listed in PDB file
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Key reference
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Title
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Probing the function of heme distortion in the h-Nox family.
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Authors
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C.Olea,
E.M.Boon,
P.Pellicena,
J.Kuriyan,
M.A.Marletta.
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Ref.
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Acs Chem Biol, 2008,
3,
703-710.
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PubMed id
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Abstract
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Hemoproteins carry out diverse functions utilizing a wide range of chemical
reactivity while employing the same heme prosthetic group. It is clear from
high-resolution crystal structures and biochemical studies that protein-bound
hemes are not planar and adopt diverse conformations. The crystal structure of
an H-NOX domain from Thermoanaerobacter tengcongensis (Tt H-NOX) contains the
most distorted heme reported to date. In this study, Tt H-NOX was engineered to
adopt a flatter heme by mutating proline 115, a conserved residue in the H-NOX
family, to alanine. Decreasing heme distortion in Tt H-NOX increases affinity
for oxygen and decreases the reduction potential of the heme iron. Additionally,
flattening the heme is associated with significant shifts in the N-terminus of
the protein. These results show a clear link between the heme conformation and
Tt H-NOX structure and demonstrate that heme distortion is an important
determinant for maintaining biochemical properties in H-NOX proteins.
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