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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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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.3.1.1.74
- cutinase.
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Reaction:
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cutin + H2O = cutin monomers
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Proteins
26:442-458
(1996)
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PubMed id:
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Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants.
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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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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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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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K.Payne,
Q.Sun,
J.Sacchettini,
and
G.F.Hatfull
(2009).
Mycobacteriophage Lysin B is a novel mycolylarabinogalactan esterase.
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Mol Microbiol,
73,
367-381.
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PDB code:
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M.P.Nyon,
D.W.Rice,
J.M.Berrisford,
H.Huang,
A.J.Moir,
C.J.Craven,
S.Nathan,
N.M.Mahadi,
and
F.D.Abu Bakar
(2008).
Crystallization and preliminary X-ray analysis of recombinant Glomerella cingulata cutinase.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
504-508.
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R.Bonasio,
C.V.Carman,
E.Kim,
P.T.Sage,
K.R.Love,
T.R.Mempel,
T.A.Springer,
and
U.H.von Andrian
(2007).
Specific and covalent labeling of a membrane protein with organic fluorochromes and quantum dots.
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Proc Natl Acad Sci U S A,
104,
14753-14758.
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I.Bertini,
V.Calderone,
M.Cosenza,
M.Fragai,
Y.M.Lee,
C.Luchinat,
S.Mangani,
B.Terni,
and
P.Turano
(2005).
Conformational variability of matrix metalloproteinases: beyond a single 3D structure.
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Proc Natl Acad Sci U S A,
102,
5334-5339.
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PDB codes:
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N.M.Micaelo,
V.H.Teixeira,
A.M.Baptista,
and
C.M.Soares
(2005).
Water dependent properties of cutinase in nonaqueous solvents: a computational study of enantioselectivity.
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Biophys J,
89,
999.
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X.Zhu,
N.A.Larsen,
A.Basran,
N.C.Bruce,
and
I.A.Wilson
(2003).
Observation of an arsenic adduct in an acetyl esterase crystal structure.
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J Biol Chem,
278,
2008-2014.
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PDB codes:
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C.D.Hodneland,
Y.S.Lee,
D.H.Min,
and
M.Mrksich
(2002).
Selective immobilization of proteins to self-assembled monolayers presenting active site-directed capture ligands.
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Proc Natl Acad Sci U S A,
99,
5048-5052.
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S.J.Ackerman,
L.Liu,
M.A.Kwatia,
M.P.Savage,
D.D.Leonidas,
G.J.Swaminathan,
and
K.R.Acharya
(2002).
Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion.
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J Biol Chem,
277,
14859-14868.
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PDB codes:
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A.Roussel,
S.Spinelli,
S.Déret,
J.Navaza,
P.Aucouturier,
and
C.Cambillau
(1999).
The structure of an entire noncovalent immunoglobulin kappa light-chain dimer (Bence-Jones protein) reveals a weak and unusual constant domains association.
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Eur J Biochem,
260,
192-199.
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PDB code:
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E.Y.Lau,
and
T.C.Bruice
(1999).
Consequences of breaking the Asp-His hydrogen bond of the catalytic triad: effects on the structure and dynamics of the serine esterase cutinase.
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Biophys J,
77,
85-98.
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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
code is
shown on the right.
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Links
