Crystallization and preliminary crystallographic analysis ofD-alanine-D-alanine ligase fromStreptococcus mutans
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چکیده
منابع مشابه
Crystallization and preliminary X-ray analysis of a D-alanyl-D-alanine ligase (EcDdlB) from Escherichia coli.
A recombinant form of Escherichia coli DdlB (EcDdlB) has been prepared and cocrystallized with ADP and D-alanyl-D-alanine to represent the ternary complex of EcDdlB. Furthermore, EcDdlB has been cocrystallized under the same conditions with the ligands ATP and D-alanyl-D-alanine, representing the product-inhibited complex. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell param...
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Streptococcus mutans dextranase hydrolyzes the internal α-1,6-linkages of dextran and belongs to glycoside hydrolase family 66. An N- and C-terminal deletion mutant of S. mutans dextranase was crystallized by the sitting-drop vapour-diffusion method. The crystals diffracted to a resolution of 1.6 Å and belonged to space group P2(1), with unit-cell parameters a = 53.2, b = 89.7, c = 63.3 Å, β = ...
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A 1.2 kb BamHI fragment from pDK30 [Robinson, Kenan, Sweeney & Donachie (1986) J. Bacteriol. 167, 809-817] was cloned in pDOC55 [O'Connor & Timmis (1987) J. Bacteriol. 169, 4457-4482] to give two constructs, pDOC89 and pDOC87, in which the Escherichia coli D-alanine:D-alanine ligase (EC 6.3.2.4) gene (ddl) was placed under the control of the lac and lambda PL promoters respectively. Both constr...
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The enzymatic incorporation of D-alanine into membranes of Lacfobacillus casei (ATCC 7469) is described. The activity is dependent on ATP, supernatant fraction and membrane fragments; it is enhanced by the addition of Mg2+. The incorporation is insensitive to ribonuclease. The product of this reaction is characterized as a hydroxylamine (1 M, pH 7.0, 37”) labile ester that is not extracted into...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section F Structural Biology and Crystallization Communications
سال: 2007
ISSN: 1744-3091
DOI: 10.1107/s1744309107040298