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PDBsum entry 1jiy
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* Residue conservation analysis
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Enzyme class:
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E.C.3.2.1.17
- lysozyme.
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Reaction:
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Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.
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DOI no:
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Acta Crystallogr D Biol Crystallogr
57:1614-1620
(2001)
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PubMed id:
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The effect of stabilizing additives on the structure and hydration of proteins: a study involving tetragonal lysozyme.
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S.Datta,
B.K.Biswal,
M.Vijayan.
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ABSTRACT
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In order to elucidate the effect of stabilizing additives on the structure of
proteins and the associated ordered water molecules in the hydration shell, the
crystal structures of tetragonal lysozyme grown in the presence of sucrose,
sorbitol and trehalose have been refined. Also refined are the structures of
orthorhombic and monoclinic lysozyme grown under the conditions in which
tetragonal lysozyme is normally grown. A comparison of the two sets of
structures with the structure of native tetragonal lysozyme shows that the
effect of the additives on the structure of the protein molecule is less than
that of the normal minor changes associated with differences in molecular
packing. Surprisingly, the same is true of the effect on the hydration shell,
represented by the ordered water molecules attached to the protein. Thus, it
appears that the cause of the stabilizing effect of the additives needs to be
sought outside the immediate neighbourhood of the protein molecule. Sorbitol and
trehalose do not coherently interact with the protein. One sucrose molecule
binds at the active-site cleft of the enzyme.
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Selected figure(s)
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Figure 3.
Figure 3 Schematic representation of the interactions of sucrose
with the enzyme molecule. This figure was prepared using LIGPLOT
(Wallace et al., 1995[Wallace, A. C., Laskowski, R. A. &
Thornton, J. M. (1995). Protein Eng. 8, 127-134.]).
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2001,
57,
1614-1620)
copyright 2001.
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Figure was
selected
by an automated process.
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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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C.C.Chang,
X.C.Yeh,
H.T.Lee,
P.Y.Lin,
and
L.S.Kan
(2004).
Refolding of lysozyme by quasistatic and direct dilution reaction paths: a first-order-like state transition.
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Phys Rev E Stat Nonlin Soft Matter Phys,
70,
011904.
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R.D.Lins,
C.S.Pereira,
and
P.H.Hünenberger
(2004).
Trehalose-protein interaction in aqueous solution.
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Proteins,
55,
177-186.
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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.
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