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1e40
From Proteopedia
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==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10924103 10924103] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10924103 10924103] | ||
| + | [[Category: Alpha-amylase]] | ||
[[Category: Bacillus amyloliquefaciens]] | [[Category: Bacillus amyloliquefaciens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tris]] | [[Category: tris]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:01:11 2007'' |
Revision as of 07:56, 30 October 2007
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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
Page seeded by OCA on Tue Oct 30 10:01:11 2007
Categories: Alpha-amylase | Bacillus amyloliquefaciens | Single protein | Bisgaard-Frantzen, H. | Borchert, T.V. | Brzozowski, A.M. | Dauter, Z. | Davies, G.J. | Lawson, D.M. | Svendsen, A. | Turkenburg, J.P. | Wilson, K.S. | CA | NA | TRS | Amylase | Complex | Family 13 | Hydrolase | Maltotriose | Tris
