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PDBsum entry 1ab1
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Plant seed protein
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PDB id
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1ab1
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References listed in PDB file
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Key reference
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Title
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Crystal structure of ser-22/ile-25 form crambin confirms solvent, Side chain substate correlations.
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Authors
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A.Yamano,
N.H.Heo,
M.M.Teeter.
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Ref.
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J Biol Chem, 1997,
272,
9597-9600.
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PubMed id
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Abstract
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It is not agreed that correlated positions of disordered protein side chains
(substate correlations) can be deduced from diffraction data. The pure
Ser-22/Ile-25 (SI form) crambin crystal structure confirms correlations deduced
for the natural, mixed sequence form of crambin crystals. Physical separation of
the mixed form into pure SI form and Pro-22/Leu-25 (PL form) crambin and the PL
form crystal structure determination (Yamano, A., and Teeter, M. M. (1994) J.
Biol. Chem. 269, 13956-13965) support the proposed (Teeter, M. M., Roe, S. M.,
and Heo, N. H. (1993) J. Mol. Biol. 230, 292-311) correlation model. Electron
density of mixed form crambin crystals shows four possible pairs of side chain
conformations for heterogeneous residue 22 and nearby Tyr-29 (2(2) = 4, two
conformations for each of two side chains). One combination can be eliminated
because of short van der Waals' contacts. However, only two alternates have been
postulated to exist in mixed form crambin: Pro-22/Tyr-29A and Ser-22/Tyr-29B. In
crystals of the PL form, Pro-22 and Tyr-29A are found to be in direct van der
Waals' contact (Yamano, A., and Teeter, M. M. (1994) J. Biol. Chem. 269,
13956-13965). Comparison of the SI form structure with the mixed form electron
density confirms that the fourth combination of side chains does not occur and
that side chain correlations are mediated by water networks.
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