Crystallization and preliminary X-ray analysis of Streptococcus mutans dextran glucosidase.

نویسندگان

  • Wataru Saburi
  • Hironori Hondoh
  • Hideaki Unno
  • Masayuki Okuyama
  • Haruhide Mori
  • Toshitaka Nakada
  • Yoshiki Matsuura
  • Atsuo Kimura
چکیده

Dextran glucosidase from Streptococcus mutans is an exo-hydrolase that acts on the nonreducing terminal alpha-1,6-glucosidic linkage of oligosaccharides and dextran with a high degree of transglucosylation. Based on amino-acid sequence similarity, this enzyme is classified into glycoside hydrolase family 13. Recombinant dextran glucosidase was purified and crystallized by the hanging-drop vapour-diffusion technique using polyethylene glycol 6000 as a precipitant. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 72.72, b = 86.47, c = 104.30 A. A native data set was collected to 2.2 A resolution from a single crystal.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Crystallization and preliminary crystallographic analysis of dextranase from Streptococcus mutans.

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 = ...

متن کامل

Calcium ion-dependent increase in thermostability of dextran glucosidase from Streptococcus mutans.

Dextran glucosidase from Streptococcus mutans (SmDG), which belongs to glycoside hydrolase family 13 (GH13), hydrolyzes the non-reducing terminal glucosidic linkage of isomaltooligosaccharides and dextran. Thermal deactivation of SmDG did not follow the single exponential decay but rather the two-step irreversible deactivation model, which involves an active intermediate having 39% specific act...

متن کامل

Structural elements responsible for the glucosidic linkage-selectivity of a glycoside hydrolase family 13 exo-glucosidase.

Glycoside hydrolase family 13 contains exo-glucosidases specific for α-(1→4)- and α-(1→6)-linkages including α-glucosidase, oligo-1,6-glucosidase, and dextran glucosidase. The α-(1→6)-linkage selectivity of Streptococcus mutans dextran glucosidase was altered to α-(1→4)-linkage selectivity through site-directed mutations at Val195, Lys275, and Glu371. V195A showed 1300-fold higher kcat/Km for m...

متن کامل

Purification, crystallization and preliminary X-ray diffraction analysis of RafE, a sugar-binding lipoprotein from Streptococcus pneumoniae

Streptococcus pneumoniae contains a large number of sugar-transport systems and the system responsible for raffinose uptake has recently been identified. The substrate-binding protein component of this system shares strong sequence homology with the multiple sugar metabolism substrate-binding protein MsmE from S. mutans and contains a lipoprotein-attachment site at cysteine residue 23. A trunca...

متن کامل

Dextran-induced agglutination of Streptococcus mutans, and its potential role in the formation of microbial dental plaques.

Glucose-grown washed cells of streptococci similar to Streptococcus mutans, which contain cell-bound dextransucrase, have been observed to agglutinate upon the addition of high molecular weight dextran. Low molecular weight dextran or unrelated polysaccharides were ineffective. Agglutination also occurred upon addition of sucrose, which can be converted into dextran, but not with other mono- an...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Acta crystallographica. Section F, Structural biology and crystallization communications

دوره 63 Pt 9  شماره 

صفحات  -

تاریخ انتشار 2007