1WL7

Structure of the thermostable arabinanase

Summary for 1WL7

• Entry DOI: 10.2210/pdb1wl7/pdb
• Descriptor: arabinanase-TS, CALCIUM ION (3 entities in total)
• Functional Keywords: arabinanase, abn-ts, thermostable enzyme, glycoside hydrolase, bacillus, hydrolase
• Biological source: Geobacillus thermodenitrificans
• Total number of polymer chains: 1
• Total formula weight: 35396.47

Authors

Yamaguchi, A.,Tada, T.,Nakaniwa, T.,Kitatani, T. (deposition date: 2004-06-21, release date: 2005-06-21, Last modification date: 2024-10-30)

Primary citation

Yamaguchi, A.,Tada, T.,Wada, K.,Nakaniwa, T.,Kitatani, T.,Sogabe, Y.,Takao, M.,Sakai, T.,Nishimura, K.
Structural basis for thermostability of endo-1,5-alpha-L-arabinanase from Bacillus thermodenitrificans TS-3.
J.Biochem.(Tokyo), 137:587-592, 2005

PubMed Abstract: The crystal structure of a thermostable endo-1,5-alpha-L-arabinanase, ABN-TS, from Bacillus thermodenitrificans TS-3 was determined at 1.9 A to an R-factor of 18.3% and an R-free-factor of 22.5%. The enzyme molecule has a five-bladed beta-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 beta-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.

PubMed: 15944411
DOI: 10.1093/jb/mvi078

Experimental method

X-RAY DIFFRACTION (1.9 Å)