1bza
From Proteopedia
(New page: 200px<br /> <applet load="1bza" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bza, resolution 1.8Å" /> '''BETA-LACTAMASE TOHO-...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1BZA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BZA OCA]]. | + | 1BZA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BZA OCA]]. |
==Reference== | ==Reference== | ||
Crystal structure of the E166A mutant of extended-spectrum beta-lactamase Toho-1 at 1.8 A resolution., Ibuka A, Taguchi A, Ishiguro M, Fushinobu S, Ishii Y, Kamitori S, Okuyama K, Yamaguchi K, Konno M, Matsuzawa H, J Mol Biol. 1999 Feb 5;285(5):2079-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9925786 9925786] | Crystal structure of the E166A mutant of extended-spectrum beta-lactamase Toho-1 at 1.8 A resolution., Ibuka A, Taguchi A, Ishiguro M, Fushinobu S, Ishii Y, Kamitori S, Okuyama K, Yamaguchi K, Konno M, Matsuzawa H, J Mol Biol. 1999 Feb 5;285(5):2079-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9925786 9925786] | ||
| + | [[Category: Beta-lactamase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:30:51 2007'' |
Revision as of 10:26, 30 October 2007
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BETA-LACTAMASE TOHO-1 FROM ESCHERICHIA COLI TUH12191
Overview
Bacterial resistance to beta-lactams is mainly due to the production of, beta-lactamase. Especially through the production of extended-spectrum, beta-lactamases (ESBLs), bacteria have acquired resistance not only to, penicillins, but also to expanded-spectrum cephems. Here, we describe the, crystal structure of the E166A mutant of class A beta-lactamase Toho-1 at, 1.8 A resolution, the first reported tertiary structure of an ESBL., Instead of the wild-type enzyme, a mutant Toho-1, in which Glu166 was, replaced with alanine, was used for this study, because of the strong, tendency of the wild-type enzyme to form twinned crystals. The overall, structure of Toho-1 is similar to the crystal structures of non-ESBLs, with no pronounced backbone rearrangement of the framework. However, there, ... [(full description)]
About this Structure
1BZA is a [Single protein] structure of sequence from [Escherichia coli] with SO4 as [ligand]. Active as [Beta-lactamase], with EC number [3.5.2.6]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the E166A mutant of extended-spectrum beta-lactamase Toho-1 at 1.8 A resolution., Ibuka A, Taguchi A, Ishiguro M, Fushinobu S, Ishii Y, Kamitori S, Okuyama K, Yamaguchi K, Konno M, Matsuzawa H, J Mol Biol. 1999 Feb 5;285(5):2079-87. PMID:9925786
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