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PDBsum entry 1nuc
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* Residue conservation analysis
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Enzyme class:
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E.C.3.1.31.1
- micrococcal nuclease.
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Reaction:
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Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.
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DOI no:
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Protein Sci
5:1026-1031
(1996)
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PubMed id:
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Mobile unnatural amino acid side chains in the core of staphylococcal nuclease.
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R.Wynn,
P.C.Harkins,
F.M.Richards,
R.O.Fox.
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ABSTRACT
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The structures of several variants of staphylococcal nuclease with long flexible
unnatural amino acid side chains in the hydrophobic core have been determined by
X-ray crystallography. The unnatural amino acids are disulfide moieties between
the lone cysteine residue in V23C nuclease and methane, ethane, 1-n-propane,
1-n-butane, 1-n-pentane, and 2-hydroxyethyl thiols. We have examined changes in
the core packing of these mutants. Side chains as large as the 1-n-propyl
cysteine disulfide can be incorporated without perturbation of the structure.
This is due, in part, to cavities present in the wild-type protein. The longest
side chains are not well defined, even though they remain buried within the
protein interior. These results suggest that the enthalpy-entropy balance that
governs the rigidity of protein interiors favors tight packing only weakly.
Additionally, the tight packing observed normally in protein interiors may
reflect, in part, the limited numbers of rotamers available to the natural amino
acids.
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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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Z.Guo,
D.Cascio,
K.Hideg,
T.Kálái,
and
W.L.Hubbell
(2007).
Structural determinants of nitroxide motion in spin-labeled proteins: tertiary contact and solvent-inaccessible sites in helix G of T4 lysozyme.
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Protein Sci,
16,
1069-1086.
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PDB codes:
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J.Zhang,
Y.Chen,
R.Chen,
and
J.Liang
(2004).
Importance of chirality and reduced flexibility of protein side chains: a study with square and tetrahedral lattice models.
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J Chem Phys,
121,
592-603.
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G.DeSantis,
P.Berglund,
M.R.Stabile,
M.Gold,
and
J.B.Jones
(1998).
Site-directed mutagenesis combined with chemical modification as a strategy for altering the specificity of the S1 and S1' pockets of subtilisin Bacillus lentus.
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Biochemistry,
37,
5968-5973.
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K.J.Frye,
and
C.A.Royer
(1998).
Probing the contribution of internal cavities to the volume change of protein unfolding under pressure.
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Protein Sci,
7,
2217-2222.
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G.Raghunathan,
and
R.L.Jernigan
(1997).
Ideal architecture of residue packing and its observation in protein structures.
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Protein Sci,
6,
2072-2083.
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R.O'Brien,
R.Wynn,
P.C.Driscoll,
B.Davis,
K.W.Plaxco,
J.M.Sturtevant,
and
J.E.Ladbury
(1997).
The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions.
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Protein Sci,
6,
1325-1332.
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R.Wynn,
P.C.Harkins,
F.M.Richards,
and
R.O.Fox
(1997).
Comparison of straight chain and cyclic unnatural amino acids embedded in the core of staphylococcal nuclease.
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Protein Sci,
6,
1621-1626.
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PDB codes:
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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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Links
