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PDBsum entry 1kxx
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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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J Biochem (tokyo)
121:1076-1081
(1997)
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PubMed id:
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Analysis of the stabilization of hen lysozyme by helix macrodipole and charged side chain interaction.
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H.Motoshima,
S.Mine,
K.Masumoto,
Y.Abe,
H.Iwashita,
Y.Hashimoto,
Y.Chijiiwa,
T.Ueda,
T.Imoto.
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ABSTRACT
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In the N-terminal region of the alpha-helix of the c-type lysozymes, two Asx
residues exist at the 18th and 27th positions. Hen lysozyme has Asp18/Asn27
(18D/27N), and we prepared three mutant lysozymes, Asn18/Asn27 (18N/27N),
Asn18/Asp27 (18N/27D), and Asp18/Asp27 (18D/27D). The stability of the wild-type
(18D/27N) lysozyme supported the existence of a hydrogen bond between the side
chain of Asp18 and the amide group at the N1 position in the alpha-helix, while
the stability of the 18N/27D lysozyme supported the presence of the capping box
between the Ser24 (N-cap) and Asp27 residues. Although electrostatic repulsion
was observed between Asp18 and Asp27 residues in 18D/27D lysozyme, the
dissociation of each residue contributed to stabilizing the B-helix in 18D/27D
lysozyme through hydrogen bonding and charge-helix macrodipole interaction. This
is the first evidence that two neighboring negative charges at the N-terminus of
the helix both increased the stability of the protein.
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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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M.Allaire,
N.Moiseeva,
C.E.Botez,
M.A.Engel,
and
P.W.Stephens
(2009).
On the possibility of using polycrystalline material in the development of structure-based generic assays.
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Acta Crystallogr D Biol Crystallogr,
65,
379-382.
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A.Harada,
H.Yagi,
A.Saito,
H.Azakami,
and
A.Kato
(2007).
Relationship between the stability of hen egg-white lysozymes mutated at sites designed to interact with alpha-helix dipoles and their secretion amounts in yeast.
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Biosci Biotechnol Biochem,
71,
2952-2961.
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M.Oda,
S.Uchiyama,
C.V.Robinson,
K.Fukui,
Y.Kobayashi,
and
T.Azuma
(2006).
Regional and segmental flexibility of antibodies in interaction with antigens of different size.
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FEBS J,
273,
1476-1487.
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M.Muraki,
and
K.Harata
(2003).
X-ray structural analysis of the ligand-recognition mechanism in the dual-affinity labeling of c-type lysozyme with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine.
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J Mol Recognit,
16,
72-82.
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PDB codes:
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R.B.Von Dreele
(2001).
Binding of N-acetylglucosamine to chicken egg lysozyme: a powder diffraction study.
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Acta Crystallogr D Biol Crystallogr,
57,
1836-1842.
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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
