Abstract：
:Endoglucanase Cel6A from Thermobifida fusca hydrolyzes the beta-1,4 linkages in cellulose at accessible points along the polymer. The structure of the catalytic domain of Cel6A from T. fusca in complex with a nonhydrolysable substrate analogue that acts as an inhibitor, methylcellobiosyl-4-thio-beta-cellobioside (Glc(2)-S-Glc(2)), has been determined to 1.5 A resolution. The glycosyl unit in subsite -1 was sterically hindered by Tyr73 and forced into a distorted (2)S(o) conformation. In the enzyme where Tyr73 was mutated to a serine residue, the hindrance was removed and the glycosyl unit in subsite -1 had a relaxed (4)C(1) chair conformation. The relaxed conformation was seen in two complex structures of the mutated enzyme, with cellotetrose (Glc(4)) at 1.64 A and Glc(2)-S-Glc(2) at 1.04 A resolution.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Larsson AM,Bergfors T,Dultz E,Irwin DC,Roos A,Driguez H,Wilson DB,Jones TAdoi
10.1021/bi0506730subject
Has Abstractpub_date
2005-10-04 00:00:00pages
12915-22issue
39eissn
0006-2960issn
1520-4995journal_volume
44pub_type
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