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PDBsum entry 2z6f
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Heme binding protein
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PDB id
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2z6f
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References listed in PDB file
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Key reference
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Title
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Structural basis for multimeric heme complexation through a specific protein-Heme interaction: the case of the third neat domain of isdh from staphylococcus aureus.
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Authors
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M.Watanabe,
Y.Tanaka,
A.Suenaga,
M.Kuroda,
M.Yao,
N.Watanabe,
F.Arisaka,
T.Ohta,
I.Tanaka,
K.Tsumoto.
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Ref.
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J Biol Chem, 2008,
283,
28649-28659.
[DOI no: ]
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PubMed id
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Abstract
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To elucidate the heme acquisition system in pathogenic bacteria, we investigated
the heme-binding properties of the third NEAT domain of IsdH (IsdH-NEAT3), a
receptor for heme located on the surfaces of pathogenic bacterial cells, by
using x-ray crystallography, isothermal titration calorimetry, examination of
absorbance spectra, mutation analysis, size-exclusion chromatography, and
analytical ultracentrifugation. We found the following: 1) IsdH-NEAT3 can bind
with multiple heme molecules by two modes; 2) heme was bound at the surface of
IsdH-NEAT3; 3) candidate residues proposed from the crystal structure were not
essential for binding with heme; and 4) IsdH-NEAT3 was associated into a
multimeric heme complex by the addition of excess heme. From these observations,
we propose a heme-binding mechanism for IsdH-NEAT3 that involves multimerization
and discuss the biological importance of this mechanism.
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Figure 4.
Comparison of residues around heme. A, IsdH-NEAT3. B,
IsdA-NEAT (Protein Data Bank code 2ITF). C, IsdC-NEAT (Protein
Data Bank code 2O6P). The bound heme molecules are shown as
sticks, with pink carbons; the heme irons appear as orange
balls. Residues coordinating heme iron and located around the
heme are also shown as sticks; their carbons are shown as green.
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Figure 8.
Schematic representation of proposed mechanism of heme
binding by IsdH-NEAT3. IsdH-NEAT3 and heme are shown as CPK
space filling model and red stick model, respectively. The
primary and secondary modes of heme binding described in the
text are indicated.
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The above figures are
reprinted
from an Open Access publication published by the ASBMB:
J Biol Chem
(2008,
283,
28649-28659)
copyright 2008.
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