1zkj

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[[Image:1zkj.gif|left|200px]]<br /><applet load="1zkj" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zkj.gif|left|200px]]
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caption="1zkj, resolution 1.55&Aring;" />
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'''Structural Basis for the Extended Substrate Spectrum of CMY-10, a Plasmid-Encoded Class C beta-lactamase'''<br />
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{{Structure
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|PDB= 1zkj |SIZE=350|CAPTION= <scene name='initialview01'>1zkj</scene>, resolution 1.55&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''Structural Basis for the Extended Substrate Spectrum of CMY-10, a Plasmid-Encoded Class C beta-lactamase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ZKJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_aerogenes Enterobacter aerogenes] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1ZKJ OCA].
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1ZKJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_aerogenes Enterobacter aerogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZKJ OCA].
==Reference==
==Reference==
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Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase., Kim JY, Jung HI, An YJ, Lee JH, Kim SJ, Jeong SH, Lee KJ, Suh PG, Lee HS, Lee SH, Cha SS, Mol Microbiol. 2006 May;60(4):907-16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16677302 16677302]
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Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase., Kim JY, Jung HI, An YJ, Lee JH, Kim SJ, Jeong SH, Lee KJ, Suh PG, Lee HS, Lee SH, Cha SS, Mol Microbiol. 2006 May;60(4):907-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16677302 16677302]
[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
[[Category: Enterobacter aerogenes]]
[[Category: Enterobacter aerogenes]]
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[[Category: plasmid]]
[[Category: plasmid]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:36:42 2008''

Revision as of 13:36, 20 March 2008


PDB ID 1zkj

Drag the structure with the mouse to rotate
, resolution 1.55Å
Ligands: and
Activity: Beta-lactamase, with EC number 3.5.2.6
Coordinates: save as pdb, mmCIF, xml



Structural Basis for the Extended Substrate Spectrum of CMY-10, a Plasmid-Encoded Class C beta-lactamase


Overview

The emergence and dissemination of extended-spectrum (ES) beta-lactamases induce therapeutic failure and a lack of eradication of clinical isolates even by third-generation beta-lactam antibiotics like ceftazidime. CMY-10 is a plasmid-encoded class C beta-lactamase with a wide spectrum of substrates. Unlike the well-studied class C ES beta-lactamase from Enterobacter cloacae GC1, the Omega-loop does not affect the active site conformation and the catalytic activity of CMY-10. Instead, a three-amino-acid deletion in the R2-loop appears to be responsible for the ES activity of CMY-10. According to the crystal structure solved at 1.55 A resolution, the deletion significantly widens the R2 active site, which accommodates the R2 side-chains of beta-lactam antibiotics. This observation led us to demonstrate the hydrolysing activity of CMY-10 towards imipenem with a long R2 substituent. The forced mutational analyses of P99 beta-lactamase reveal that the introduction of deletion mutations into the R2-loop is able to extend the substrate spectrum of class C non-ES beta-lactamases, which is compatible with the isolation of natural class C ES enzymes harbouring deletion mutations in the R2-loop. Consequently, the opening of the R2 active site by the deletion of some residues in the R2-loop can be considered as an operative molecular strategy of class C beta-lactamases to extend their substrate spectrum.

About this Structure

1ZKJ is a Single protein structure of sequence from Enterobacter aerogenes. Full crystallographic information is available from OCA.

Reference

Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase., Kim JY, Jung HI, An YJ, Lee JH, Kim SJ, Jeong SH, Lee KJ, Suh PG, Lee HS, Lee SH, Cha SS, Mol Microbiol. 2006 May;60(4):907-16. PMID:16677302

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