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1ll5
From Proteopedia
(New page: 200px<br /><applet load="1ll5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ll5, resolution 1.80Å" /> '''X-ray crystal struct...) |
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| - | [[Image:1ll5.gif|left|200px]]<br /><applet load="1ll5" size=" | + | [[Image:1ll5.gif|left|200px]]<br /><applet load="1ll5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ll5, resolution 1.80Å" /> | caption="1ll5, resolution 1.80Å" /> | ||
'''X-ray crystal structure of AmpC WT beta-lactamase in complex with covalently bound imipenem'''<br /> | '''X-ray crystal structure of AmpC WT beta-lactamase in complex with covalently bound imipenem'''<br /> | ||
==Overview== | ==Overview== | ||
| - | To determine how imipenem inhibits the class C beta-lactamase AmpC, the | + | To determine how imipenem inhibits the class C beta-lactamase AmpC, the X-ray crystal structure of the acyl-enzyme complex was determined to a resolution of 1.80 A. In the complex, the lactam carbonyl oxygen of imipenem has flipped by approximately 180 degrees compared to its expected position; the electrophilic acyl center is thus displaced from the point of hydrolytic attack. This conformation resembles that of imipenem bound to the class A enzyme TEM-1 but is different from that of moxalactam bound to AmpC. |
==About this Structure== | ==About this Structure== | ||
| - | 1LL5 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 IM2 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] Full crystallographic information is available from [http:// | + | 1LL5 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 <scene name='pdbligand=IM2:'>IM2</scene> 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LL5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Beadle, B | + | [[Category: Beadle, B M.]] |
| - | [[Category: Shoichet, B | + | [[Category: Shoichet, B K.]] |
[[Category: IM2]] | [[Category: IM2]] | ||
[[Category: beta-lactamase]] | [[Category: beta-lactamase]] | ||
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[[Category: imipenem]] | [[Category: imipenem]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:57 2008'' |
Revision as of 11:45, 21 February 2008
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X-ray crystal structure of AmpC WT beta-lactamase in complex with covalently bound imipenem
Overview
To determine how imipenem inhibits the class C beta-lactamase AmpC, the X-ray crystal structure of the acyl-enzyme complex was determined to a resolution of 1.80 A. In the complex, the lactam carbonyl oxygen of imipenem has flipped by approximately 180 degrees compared to its expected position; the electrophilic acyl center is thus displaced from the point of hydrolytic attack. This conformation resembles that of imipenem bound to the class A enzyme TEM-1 but is different from that of moxalactam bound to AmpC.
About this Structure
1LL5 is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
Reference
Structural basis for imipenem inhibition of class C beta-lactamases., Beadle BM, Shoichet BK, Antimicrob Agents Chemother. 2002 Dec;46(12):3978-80. PMID:12435704
Page seeded by OCA on Thu Feb 21 13:45:57 2008
