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PDBsum entry 1cuc
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Hydrolase (serine esterase)
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PDB id
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1cuc
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References listed in PDB file
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Key reference
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Title
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Dynamics of fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants.
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Authors
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S.Longhi,
A.Nicolas,
L.Creveld,
M.Egmond,
C.T.Verrips,
J.De vlieg,
C.Martinez,
C.Cambillau.
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Ref.
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Proteins, 1996,
26,
442-458.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
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Abstract
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In characterizing mutants and covalently inhibited complexes of Fusarium solani
cutinase, which is a 197-residue lipolytic enzyme, 34 variant structures,
crystallizing in 8 different crystal forms, have been determined, mostly at high
resolution. Taking advantage of this considerable body of information, a
structural comparative analysis was carried out to investigate the dynamics of
cutinase. Surface loops were identified as the major flexible protein regions,
particularly those forming the active-site groove, whereas the elements
constituting the protein scaffold were found to retain the same conformation in
all the cutinase variants studied. Flexibility turned out to be correlated with
thermal motion. With a given crystal packing environment, a high flexibility
turned out to be correlated with a low involvement in crystal packing contacts.
The high degree of crystal polymorphism, which allowed different conformations
with similar energy to be detected, made it possible to identify motions which
would have remained unidentified if only a single crystal form had been
available. Fairly good agreement was found to exist between the data obtained
from the structural comparison and those from a molecular dynamics (MD)
simulation carried out on the native enzyme. The crystallographic approach used
in this study turned out to be a suitable tool for investigating cutinase
dynamics. Because of the availability of a set of closely related proteins in
different crystal environments, the intrinsic drawback of a crystallographic
approach was bypassed. By combining several static pictures, the dynamics of the
protein could be monitored much more realistically than what can be achieved on
the basis of static pictures alone.
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Secondary reference #1
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Title
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Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state.
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Authors
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A.Nicolas,
M.Egmond,
C.T.Verrips,
J.De vlieg,
S.Longhi,
C.Cambillau,
C.Martinez.
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Ref.
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Biochemistry, 1996,
35,
398-410.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
87%.
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Secondary reference #2
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Title
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Cutinase, A lipolytic enzyme with a preformed oxyanion hole.
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Authors
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C.Martinez,
A.Nicolas,
H.Van tilbeurgh,
M.P.Egloff,
C.Cudrey,
R.Verger,
C.Cambillau.
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Ref.
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Biochemistry, 1994,
33,
83-89.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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Engineering cysteine mutants to obtain crystallographic phases with a cutinase from fusarium solani pisi.
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Authors
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C.Martinez,
P.De geus,
P.Stanssens,
M.Lauwereys,
C.Cambillau.
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Ref.
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Protein Eng, 1993,
6,
157-165.
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PubMed id
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Secondary reference #4
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Title
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Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent.
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Authors
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C.Martinez,
P.De geus,
M.Lauwereys,
G.Matthyssens,
C.Cambillau.
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Ref.
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Nature, 1992,
356,
615-618.
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PubMed id
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