 |
PDBsum entry 5nuc
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
Mobile unnatural amino acid side chains in the core of staphylococcal nuclease.
|
|
|
Authors
|
|
R.Wynn,
P.C.Harkins,
F.M.Richards,
R.O.Fox.
|
|
|
Ref.
|
|
Protein Sci, 1996,
5,
1026-1031.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Interactions in nonnative and truncated forms of staphylococcal nuclease as indicated by mutational free energy changes.
|
|
|
Authors
|
|
R.Wynn,
C.L.Anderson,
F.M.Richards,
R.O.Fox.
|
|
|
Ref.
|
|
Protein Sci, 1995,
4,
1815-1823.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Figure 1.
Fig. 1. Ribondiagramofstaphylococcalnuclease.
ordinates ere fromHyne and Fox (1991). Thevaline
side chain at position 23 is shown n whitc. Also shown
in lack at thc Y carbon is postion 135, the last esidue
in hetruncatedforms used in this studv.
|
|
Figure 2.
Fig. 2. CD spectra. A: Full-lengthnuclease V23C variants. B: Nuc
V23C variants. a,PSH; b,methyl;cethyl; d, propyl;e,butyl;f,pen-
tyl;g,BME; h, IAC.
|
|
|
|
|
|
The above figures are
reproduced from the cited reference
which is an Open Access publication published by the Protein Society
|
|
|
Secondary reference #2
|
|
|
Title
|
|
Unnatural amino acid packing mutants of escherichia coli thioredoxin produced by combined mutagenesis/chemical modification techniques.
|
|
|
Authors
|
|
R.Wynn,
F.M.Richards.
|
|
|
Ref.
|
|
Protein Sci, 1993,
2,
395-403.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Figure 1.
Fig. 1. lpha-carbonrace of oxidized sch-
erichiacoli thioredoxin with Leu 78 and the
active-site disulfide included. Coordinates
werefromthestructure o Kattiet al. (1990).
The sheeti shown approximatelyperpen-
dicular to heviewing plane. Thehelicespro-
vidinginteriorpackingappear to the nd
above Leu 78.
|
|
Figure 4.
Fig. 4. CD of mutantproteins.
|
|
|
|
|
|
The above figures are
reproduced from the cited reference
which is an Open Access publication published by the Protein Society
|
|
|
|
|
|
|
