2bog
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CATALYTIC DOMAIN OF ENDO-1,4-GLUCANASE CEL6A MUTANT Y73S FROM THERMOBIFIDA FUSCA IN COMPLEX WITH METHYL CELLOBIOSYL-4-THIO-BETA-CELLOBIOSIDE
OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
2BOG is a [Single protein] structure of sequence from [Thermomonospora fusca]. Active as [Hydrolase], with EC number [3.2.1.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of Thermobifida fusca endoglucanase Cel6A in complex with substrate and inhibitor: the role of tyrosine Y73 in substrate ring distortion., Larsson AM, Bergfors T, Dultz E, Irwin DC, Roos A, Driguez H, Wilson DB, Jones TA, Biochemistry. 2005 Oct 4;44(39):12915-22. PMID:16185060
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