1bag

From Proteopedia

Revision as of 12:48, 30 October 2007

ALPHA-AMYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH MALTOPENTAOSE

Overview

The X-ray crystal structure of a catalytic-site mutant EQ208, [Glu208-->Gln] of alpha-amylase from Bacillus subtilis cocrystallized with, maltopentaose (G5) and acarbose has been determined by multiple, isomorphous replacement at 2.5 A resolution. Restrained crystallographic, refinement has resulted in an R-factor of 19.8% in the 7.0 to 2.5 A, resolution range. EQ208 consists of three domains containing a, (beta/alpha)8-barrel as observed in other alpha-amylases. Clear connected, density corresponding to a pentasaccharide was observed, which was, considered as the G5 molecule based on the high affinity of EQ208 for G5, that could replace pre-bound acarbose or a possible transglycosylation, product of acarbose. The conformation around the third, alpha-(1,4)-glucosidic bond makes a sharp ... [(full description)]

About this Structure

1BAG is a [Single protein] structure of sequence from [Bacillus subtilis] with CA as [ligand]. Active as [Alpha-amylase], with EC number [3.2.1.1]. Structure known Active Sites: CA1, CA2 and CA3. Full crystallographic information is available from [OCA].

Reference

Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose., Fujimoto Z, Takase K, Doui N, Momma M, Matsumoto T, Mizuno H, J Mol Biol. 1998 Mar 27;277(2):393-407. PMID:9514750

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