1wl7
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(New page: 200px<br /><applet load="1wl7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wl7, resolution 1.90Å" /> '''Structure of the the...)
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Revision as of 22:02, 24 November 2007
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Structure of the thermostable arabinanase
Overview
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.
About this Structure
1WL7 is a Single protein structure of sequence from Geobacillus thermodenitrificans with CA as ligand. Active as Arabinan endo-1,5-alpha-L-arabinosidase, with EC number 3.2.1.99 Full crystallographic information is available from OCA.
Reference
Structural basis for thermostability of endo-1,5-alpha-L-arabinanase from Bacillus thermodenitrificans TS-3., Yamaguchi A, Tada T, Wada K, Nakaniwa T, Kitatani T, Sogabe Y, Takao M, Sakai T, Nishimura K, J Biochem (Tokyo). 2005 May;137(5):587-92. PMID:15944411
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