1s6r

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(New page: 200px<br /><applet load="1s6r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s6r, resolution 2.24&Aring;" /> '''908R CLASS C BETA-LA...)
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[[Image:1s6r.gif|left|200px]]<br /><applet load="1s6r" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1s6r, resolution 2.24&Aring;" />
caption="1s6r, resolution 2.24&Aring;" />
'''908R CLASS C BETA-LACTAMASE BOUND TO IODO-ACETAMIDO-PHENYL BORONIC ACID'''<br />
'''908R CLASS C BETA-LACTAMASE BOUND TO IODO-ACETAMIDO-PHENYL BORONIC ACID'''<br />
==Overview==
==Overview==
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The structures of the class C beta-lactamase from Enterobacter cloacae, 908R alone and in complex with a boronic acid transition-state analogue, were determined by X-ray crystallography at 2.1 and 2.3 A, respectively., The structure of the enzyme resembles those of other class C, beta-lactamases. The structure of the complex with the transition-state, analogue, iodo-acetamido-phenyl boronic acid, shows that the inhibitor is, covalently bound to the active-site serine (Ser64). Binding of the, inhibitor within the active site is compared with previously determined, structures of complexes with other class C enzymes. The structure of the, boronic acid adduct indicates ways to improve the affinity of this class, of inhibitors. This structure of 908R class C beta-lactamase in complex, with a transition-state analogue provides further insights into the, mechanism of action of these hydrolases.
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The structures of the class C beta-lactamase from Enterobacter cloacae 908R alone and in complex with a boronic acid transition-state analogue were determined by X-ray crystallography at 2.1 and 2.3 A, respectively. The structure of the enzyme resembles those of other class C beta-lactamases. The structure of the complex with the transition-state analogue, iodo-acetamido-phenyl boronic acid, shows that the inhibitor is covalently bound to the active-site serine (Ser64). Binding of the inhibitor within the active site is compared with previously determined structures of complexes with other class C enzymes. The structure of the boronic acid adduct indicates ways to improve the affinity of this class of inhibitors. This structure of 908R class C beta-lactamase in complex with a transition-state analogue provides further insights into the mechanism of action of these hydrolases.
==About this Structure==
==About this Structure==
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1S6R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae] with IAP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], 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=1S6R OCA].
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1S6R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae] with <scene name='pdbligand=IAP:'>IAP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], 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=1S6R OCA].
==Reference==
==Reference==
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:59:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:33 2008''

Revision as of 12:58, 21 February 2008

Image:1s6r.gif

1s6r, resolution 2.24Å

Drag the structure with the mouse to rotate

908R CLASS C BETA-LACTAMASE BOUND TO IODO-ACETAMIDO-PHENYL BORONIC ACID

Overview

The structures of the class C beta-lactamase from Enterobacter cloacae 908R alone and in complex with a boronic acid transition-state analogue were determined by X-ray crystallography at 2.1 and 2.3 A, respectively. The structure of the enzyme resembles those of other class C beta-lactamases. The structure of the complex with the transition-state analogue, iodo-acetamido-phenyl boronic acid, shows that the inhibitor is covalently bound to the active-site serine (Ser64). Binding of the inhibitor within the active site is compared with previously determined structures of complexes with other class C enzymes. The structure of the boronic acid adduct indicates ways to improve the affinity of this class of inhibitors. This structure of 908R class C beta-lactamase in complex with a transition-state analogue provides further insights into the mechanism of action of these hydrolases.

About this Structure

1S6R is a Single protein structure of sequence from Enterobacter cloacae with as ligand. Active as Hydrolase, with EC number 3.5.2.6. Full crystallographic information is available from OCA.

Reference

Crystal structure of Enterobacter cloacae 908R class C beta-lactamase bound to iodo-acetamido-phenyl boronic acid, a transition-state analogue., Wouters J, Fonze E, Vermeire M, Frere JM, Charlier P, Cell Mol Life Sci. 2003 Aug;60(8):1764-73. PMID:14521155

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