1ome
From Proteopedia
(New page: 200px<br /> <applet load="1ome" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ome, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1OME is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]] with CL 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=1OME OCA]]. | + | 1OME is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]] with CL 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: CAT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OME OCA]]. |
==Reference== | ==Reference== | ||
Role of the omega-loop in the activity, substrate specificity, and structure of class A beta-lactamase., Banerjee S, Pieper U, Kapadia G, Pannell LK, Herzberg O, Biochemistry. 1998 Mar 10;37(10):3286-96. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9521648 9521648] | Role of the omega-loop in the activity, substrate specificity, and structure of class A beta-lactamase., Banerjee S, Pieper U, Kapadia G, Pannell LK, Herzberg O, Biochemistry. 1998 Mar 10;37(10):3286-96. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9521648 9521648] | ||
| + | [[Category: Beta-lactamase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
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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 14:29:22 2007'' |
Revision as of 12:24, 30 October 2007
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CRYSTAL STRUCTURE OF THE OMEGA LOOP DELETION MUTANT (RESIDUES 163-178 DELETED) OF BETA-LACTAMASE FROM STAPHYLOCOCCUS AUREUS PC1
Overview
The structure of class A beta-lactamases contains an omega-loop associated, with the active site, which carries a key catalytic residue, Glu166. A, 16-residue omega-loop deletion mutant of beta-lactamase from, Staphylococcus aureus PC1, encompassing residues 163-178, was produced in, order to examine the functional and structural role of the loop. The, crystal structure was determined and refined at 2.3 A, and the kinetics of, the mutant enzyme was characterized with a variety of beta-lactam, antibiotics. In general, the wild-type beta-lactamase hydrolyzes, penicillin compounds better than cephalosporins. In contrast, the deletion, of the omega-loop led to a variant enzyme that acts only on, cephalosporins, including third generation compounds. Kinetic measurements, and electrospray mass ... [(full description)]
About this Structure
1OME is a [Single protein] structure of sequence from [Staphylococcus aureus] with CL as [ligand]. Active as [Beta-lactamase], with EC number [3.5.2.6]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
Reference
Role of the omega-loop in the activity, substrate specificity, and structure of class A beta-lactamase., Banerjee S, Pieper U, Kapadia G, Pannell LK, Herzberg O, Biochemistry. 1998 Mar 10;37(10):3286-96. PMID:9521648
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