1e40

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Image:1e40.gif

1e40, resolution 2.2Å

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TRIS/MALTOTRIOSE COMPLEX OF CHIMAERIC AMYLASE FROM B. AMYLOLIQUEFACIENS AND B. LICHENIFORMIS AT 2.2A

Overview

Several chimeric alpha-amylases genes were constructed by an in vivo, recombination technique from the Bacillus amyloliquefaciens and Bacillus, licheniformis genes. One of the fusion amylases (hereafter BA2), consisting of residues 1-300 from B. amyloliquefaciens and 301-483 from B., licheniformis, has been extensively studied by X-ray crystallography at, resolutions between 2.2 and 1.7 A. The 3-dimensional structure of the, native enzyme was solved by multiple isomorphous replacement, and refined, at a resolution of 1.7 A. It consists of 483 amino acids, organized, similarly to the known B. lichiniformis alpha-amylase structure [Machius, et al. (1995) J. Mol. Biol. 246, 545-559], but features 4 bound calcium, ions. Two of these form part of a linear cluster of three ions, the, central ... [(full description)]

About this Structure

1E40 is a [Single protein] structure of sequence from [Bacillus amyloliquefaciens] with CA, NA and TRS as [ligands]. Active as [Alpha-amylase], with EC number [3.2.1.1]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].

Reference

Structural analysis of a chimeric bacterial alpha-amylase. High-resolution analysis of native and ligand complexes., Brzozowski AM, Lawson DM, Turkenburg JP, Bisgaard-Frantzen H, Svendsen A, Borchert TV, Dauter Z, Wilson KS, Davies GJ, Biochemistry. 2000 Aug 8;39(31):9099-107. PMID:10924103

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