1e3x: Difference between revisions
New page: left|200px<br /> <applet load="1e3x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e3x, resolution 1.9Å" /> '''NATIVE STRUCTURE OF ... |
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==About this Structure== | ==About this Structure== | ||
1E3X is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]] with CA and NA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E3X OCA]]. | 1E3X is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]] with CA and NA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E3X OCA]]. | ||
==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: hydrolase]] | [[Category: hydrolase]] | ||
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Revision as of 15:21, 30 October 2007
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NATIVE STRUCTURE OF CHIMAERIC AMYLASE FROM B. AMYLOLIQUEFACIENS AND B. LICHENIFORMIS AT 1.92A
OverviewOverview
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 StructureAbout this Structure
1E3X is a [Single protein] structure of sequence from [Bacillus amyloliquefaciens] with CA and NA 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].
ReferenceReference
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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