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3bls
From Proteopedia
(New page: 200px<br /> <applet load="3bls" size="450" color="white" frame="true" align="right" spinBox="true" caption="3bls, resolution 2.3Å" /> '''AMPC BETA-LACTAMASE ...) |
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==About this Structure== | ==About this Structure== | ||
| - | 3BLS 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 APB 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=3BLS OCA]]. | + | 3BLS 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 APB 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 Sites: ACB and ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3BLS OCA]]. |
==Reference== | ==Reference== | ||
Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design., Usher KC, Blaszczak LC, Weston GS, Shoichet BK, Remington SJ, Biochemistry. 1998 Nov 17;37(46):16082-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9819201 9819201] | Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design., Usher KC, Blaszczak LC, Weston GS, Shoichet BK, Remington SJ, Biochemistry. 1998 Nov 17;37(46):16082-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9819201 9819201] | ||
| + | [[Category: Beta-lactamase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: serine hydrolase]] | [[Category: serine 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 13:52:28 2007'' |
Revision as of 11:47, 30 October 2007
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AMPC BETA-LACTAMASE FROM ESCHERICHIA COLI
Overview
The structures of AmpC beta-lactamase from Escherichia coli, alone and in, complex with a transition-state analogue, have been determined by X-ray, crystallography. The native enzyme was determined to 2.0 A resolution, and, the structure with the transition-state analogue m-aminophenylboronic acid, was determined to 2.3 A resolution. The structure of AmpC from E. coli, resembles those previously determined for the class C enzymes from, Enterobacter cloacae and Citrobacter freundii. The transition-state, analogue, m-aminophenylboronic acid, makes several interactions with AmpC, that were unexpected. Perhaps most surprisingly, the putative "oxyanion", of the boronic acid forms what appears to be a hydrogen bond with the, backbone carbonyl oxygen of Ala318, suggesting that this atom is, ... [(full description)]
About this Structure
3BLS is a [Single protein] structure of sequence from [Escherichia coli] with APB as [ligand]. Active as [Beta-lactamase], with EC number [3.5.2.6]. Structure known Active Sites: ACB and ACT. Full crystallographic information is available from [OCA].
Reference
Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design., Usher KC, Blaszczak LC, Weston GS, Shoichet BK, Remington SJ, Biochemistry. 1998 Nov 17;37(46):16082-92. PMID:9819201
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