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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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Contents |
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* Residue conservation analysis
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J Biol Chem
272:9597-9600
(1997)
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PubMed id:
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Crystal structure of Ser-22/Ile-25 form crambin confirms solvent, side chain substate correlations.
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A.Yamano,
N.H.Heo,
M.M.Teeter.
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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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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F.Pavelcík,
and
J.Václavík
(2010).
Performance of phased rotation, conformation and translation function: accurate protein model building with tripeptidic and tetrapeptidic fragments.
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Acta Crystallogr D Biol Crystallogr,
66,
1012-1023.
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U.D.Ramirez,
and
D.M.Freymann
(2006).
Analysis of protein hydration in ultrahigh-resolution structures of the SRP GTPase Ffh.
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Acta Crystallogr D Biol Crystallogr,
62,
1520-1534.
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PDB codes:
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M.Vila-Perelló,
and
D.Andreu
(2005).
Characterization and structural role of disulfide bonds in a highly knotted thionin from Pyrularia pubera.
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Biopolymers,
80,
697-707.
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P.B.Pelegrini,
and
O.L.Franco
(2005).
Plant gamma-thionins: novel insights on the mechanism of action of a multi-functional class of defense proteins.
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Int J Biochem Cell Biol,
37,
2239-2253.
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B.Stec,
O.Markman,
U.Rao,
G.Heffron,
S.Henderson,
L.P.Vernon,
V.Brumfeld,
and
M.M.Teeter
(2004).
Proposal for molecular mechanism of thionins deduced from physico-chemical studies of plant toxins.
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J Pept Res,
64,
210-224.
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M.M.Teeter
(2004).
Myoglobin cavities provide interior ligand pathway.
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Protein Sci,
13,
313-318.
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M.M.Teeter,
A.Yamano,
B.Stec,
and
U.Mohanty
(2001).
On the nature of a glassy state of matter in a hydrated protein: Relation to protein function.
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Proc Natl Acad Sci U S A,
98,
11242-11247.
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PDB codes:
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C.Jelsch,
M.M.Teeter,
V.Lamzin,
V.Pichon-Pesme,
R.H.Blessing,
and
C.Lecomte
(2000).
Accurate protein crystallography at ultra-high resolution: valence electron distribution in crambin.
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Proc Natl Acad Sci U S A,
97,
3171-3176.
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PDB code:
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F.Xu,
and
T.A.Cross
(1999).
Water: foldase activity in catalyzing polypeptide conformational rearrangements.
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Proc Natl Acad Sci U S A,
96,
9057-9061.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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