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PDBsum entry 1kev
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Oxidoreductase
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PDB id
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1kev
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystalline alcohol dehydrogenases from the mesophilic bacterium clostridium beijerinckii and the thermophilic bacterium thermoanaerobium brockii: preparation, Characterization and molecular symmetry.
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Authors
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Y.Korkhin,
F.Frolow,
O.Bogin,
M.Peretz,
A.J.Kalb,
Y.Burstein.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1996,
52,
882-886.
[DOI no: ]
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PubMed id
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Abstract
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Two tetrameric NADP(+)-dependent bacterial secondary alcohol dehydrogenases have
been crystallized in the apo- and the holo-enzyme forms. Crystals of the
holo-enzyme from the mesophilic Clostridium beijerinckii (NCBAD) belong to space
group P2(1)2(1)2(1) with unit-cell dimensions a = 90.5, b = 127.9, c = 151.4 A.
Crystals of the apo-enzyme (CBAD) belong to the same space group with unit-cell
dimensions a = 80.4, b = 102.3, c = 193.5 A. Crystals of the holo-enzyme from
the thermophilic Thermoanaerobium brockii (NTBAD) belong to space group P6(1(5))
(a = b = 80.6, c = 400.7 A). Crystals of the apo-form of TBAD (point mutant
GI98D) belong to space group P2(1) with cell dimensions a = 123.0, b = 84.8, c =
160.4 A beta = 99.5 degrees. Crystals of CBAD, NCBAD and NTBAD contain one
tetramer per asymmetric unit. They diffract to 2.0 A resolution at liquid
nitrogen temperature. Crystals of TBAD(GI98D) have two tetramers per asymmetric
unit and diffract to 2.7 A at 276 K. Self-rotation analysis shows that both
enzymes are tetramers of 222 symmetry.
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Figure 2.
Fig. 2. ~= 180 ° sections of self-rotation maps for (a) CBAD; (b) (c) NTBAD and (d) TBAD (GI98D).
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1996,
52,
882-886)
copyright 1996.
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