1pio

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(New page: 200px<br /><applet load="1pio" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pio, resolution 2.8&Aring;" /> '''AN ENGINEERED STAPHYL...)
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[[Image:1pio.jpg|left|200px]]<br /><applet load="1pio" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1pio.jpg|left|200px]]<br /><applet load="1pio" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pio, resolution 2.8&Aring;" />
caption="1pio, resolution 2.8&Aring;" />
'''AN ENGINEERED STAPHYLOCOCCUS AUREUS PC1 BETA-LACTAMASE THAT HYDROLYSES THIRD GENERATION CEPHALOSPORINS'''<br />
'''AN ENGINEERED STAPHYLOCOCCUS AUREUS PC1 BETA-LACTAMASE THAT HYDROLYSES THIRD GENERATION CEPHALOSPORINS'''<br />
==Overview==
==Overview==
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The beta-lactamase from Staphylococcus aureus PC1 has been cloned into an, Escherichia coli vector for site-directed mutagenesis and high-level, protein expression. A mutant enzyme has been produced in which Ala238 is, replaced by a serine, and Ile239 is deleted (A238S:I239del). The, engineered enzyme hydrolyses third-generation cephalosporins substantially, more rapidly than the parental enzyme does, while hydrolysis of, benzylpenicillin is slower with the mutant than with the wild-type and, native enzymes. The mutant beta-lactamase has been crystallized and the, structure determined and refined at 2.8 A resolution. The disposition of, the beta-strand which forms the side of the active site is altered in, comparison with the native S. aureus beta-lactamase structure, widening, the active site cleft and providing space to accommodate the bulky, side-chains of the third-generation cephalosporins.
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The beta-lactamase from Staphylococcus aureus PC1 has been cloned into an Escherichia coli vector for site-directed mutagenesis and high-level protein expression. A mutant enzyme has been produced in which Ala238 is replaced by a serine, and Ile239 is deleted (A238S:I239del). The engineered enzyme hydrolyses third-generation cephalosporins substantially more rapidly than the parental enzyme does, while hydrolysis of benzylpenicillin is slower with the mutant than with the wild-type and native enzymes. The mutant beta-lactamase has been crystallized and the structure determined and refined at 2.8 A resolution. The disposition of the beta-strand which forms the side of the active site is altered in comparison with the native S. aureus beta-lactamase structure, widening the active site cleft and providing space to accommodate the bulky side-chains of the third-generation cephalosporins.
==About this Structure==
==About this Structure==
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1PIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PIO OCA].
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1PIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PIO OCA].
==Reference==
==Reference==
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[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Herzberg, O.]]
[[Category: Herzberg, O.]]
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[[Category: Zawadzke, L.E.]]
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[[Category: Zawadzke, L E.]]
[[Category: hydrolase (acting on cyclic amides)]]
[[Category: hydrolase (acting on cyclic amides)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:50:39 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:09 2008''

Revision as of 12:29, 21 February 2008


1pio, resolution 2.8Å

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AN ENGINEERED STAPHYLOCOCCUS AUREUS PC1 BETA-LACTAMASE THAT HYDROLYSES THIRD GENERATION CEPHALOSPORINS

Overview

The beta-lactamase from Staphylococcus aureus PC1 has been cloned into an Escherichia coli vector for site-directed mutagenesis and high-level protein expression. A mutant enzyme has been produced in which Ala238 is replaced by a serine, and Ile239 is deleted (A238S:I239del). The engineered enzyme hydrolyses third-generation cephalosporins substantially more rapidly than the parental enzyme does, while hydrolysis of benzylpenicillin is slower with the mutant than with the wild-type and native enzymes. The mutant beta-lactamase has been crystallized and the structure determined and refined at 2.8 A resolution. The disposition of the beta-strand which forms the side of the active site is altered in comparison with the native S. aureus beta-lactamase structure, widening the active site cleft and providing space to accommodate the bulky side-chains of the third-generation cephalosporins.

About this Structure

1PIO is a Single protein structure of sequence from Staphylococcus aureus. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.

Reference

An engineered Staphylococcus aureus PC1 beta-lactamase that hydrolyses third-generation cephalosporins., Zawadzke LE, Smith TJ, Herzberg O, Protein Eng. 1995 Dec;8(12):1275-85. PMID:8869640

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