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PDBsum entry 3vl3
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Oxidoreductase
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PDB id
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3vl3
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References listed in PDB file
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Key reference
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Title
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High-Pressure-Induced water penetration into 3-Isopropylmalate dehydrogenase.
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Authors
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T.Nagae,
T.Kawamura,
L.M.Chavas,
K.Niwa,
M.Hasegawa,
C.Kato,
N.Watanabe.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2012,
68,
300-309.
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PubMed id
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Abstract
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Hydrostatic pressure induces structural changes in proteins, including
denaturation, the mechanism of which has been attributed to water penetration
into the protein interior. In this study, structures of 3-isopropylmalate
dehydrogenase (IPMDH) from Shewanella oneidensis MR-1 were determined at about
2 Å resolution under pressures ranging from 0.1 to 650 MPa using a diamond
anvil cell (DAC). Although most of the protein cavities are monotonically
compressed as the pressure increases, the volume of one particular cavity at the
dimer interface increases at pressures over 340 MPa. In parallel with this
volume increase, water penetration into the cavity could be observed at
pressures over 410 MPa. In addition, the generation of a new cleft on the
molecular surface accompanied by water penetration could also be observed at
pressures over 580 MPa. These water-penetration phenomena are considered to be
initial steps in the pressure-denaturation process of IPMDH.
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