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Journal of Biochemistry 2005 137(5):587-592; doi:10.1093/jb/mvi078
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© 2005 The Japanese Biochemical Society

Regular Paper

Structural Basis for Thermostability of Endo-1,5-{alpha}-l-Arabinanase from Bacillus thermodenitrificans TS-3

Asako Yamaguchi1, Toshiji Tada1,*, Kei Wada1, Tetsuko Nakaniwa1, Tomoya Kitatani1, Yuri Sogabe1, Makoto Takao2, Takuo Sakai2 and Keiichiro Nishimura1

1 Research Institute for Advanced Science and Technology, Osaka Prefecture University, Sakai, Osaka 599-8570; and 2 IGA Bioresearch, Amagasaki, Hyogo 660-0805

* To whom correspondence should be addressed. Phone: +81-72-254-9820, Fax: +81-72-252-6776, E-mail: tada{at}b.s.osakafu-u.ac.jp

The crystal structure of a thermostable endo-1,5-{alpha}-l-arabinanase, ABN-TS, from Bacillus thermodenitrificans TS-3 was determined at 1.9 Å to an R-factor of 18.3% and an R-free-factor of 22.5%. The enzyme molecule has a five-bladed ß-propeller fold. The substrate-binding cleft formed across one face of the propeller is open on both sides to allow random binding of several sugar units in the polymeric substrate arabinan. The ß-propeller fold is stabilized through a ring closure. ABN-TS exhibits a new closure-mode involving residues in the N-terminal region: Phe7 to Gly21 exhibit hydrogen bonds and hydrophobic interactions with the first and last blades, and Phe4 links the second and third blades through a hydrogen bond and an aromatic stacking interaction, respectively. The role of the N-terminal region in the thermostability was confirmed with a mutant lacking 16 amino acid residues from the N-terminus of ABN-TS.


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