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1e3u

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[[Image:1e3u.gif|left|200px]]
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{{STRUCTURE_1e3u| PDB=1e3u | SCENE= }}
{{STRUCTURE_1e3u| PDB=1e3u | SCENE= }}
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'''MAD STRUCTURE OF OXA10 CLASS D BETA-LACTAMASE'''
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===MAD STRUCTURE OF OXA10 CLASS D BETA-LACTAMASE===
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==Overview==
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BACKGROUND: beta-lactam antibiotic therapies are commonly challenged by the hydrolytic activities of beta-lactamases in bacteria. These enzymes have been grouped into four classes: A, B, C, and D. Class B beta-lactamases are zinc dependent, and enzymes of classes A, C, and D are transiently acylated on a serine residue in the course of the turnover chemistry. While class A and C beta-lactamases have been extensively characterized by biochemical and structural methods, class D enzymes remain the least studied despite their increasing importance in the clinic. RESULTS: The crystal structure of the OXA10 class D beta-lactamase has been solved to 1.66 A resolution from a gold derivative and MAD phasing. This structure reveals that beta-lactamases from classes D and A, despite very poor sequence similarity, share a similar overall fold. An additional beta strand in OXA10 mediates the association into dimers characterized by analytical ultracentrifugation. Major differences are found when comparing the molecular details of the active site of this class D enzyme to the corresponding regions in class A and C beta-lactamases. In the native structure of the OXA10 enzyme solved to 1.8 A, Lys-70 is carbamylated. CONCLUSIONS: Several features were revealed by this study: the dimeric structure of the OXA10 beta-lactamase, an extension of the substrate binding site which suggests that class D enzymes may bind other substrates beside beta-lactams, and carbamylation of the active site Lys-70 residue. The CO2-dependent activity of the OXA10 enzyme and the kinetic properties of the natural OXA17 mutant protein suggest possible relationships between carbamylation, inhibition of the enzyme by anions, and biphasic behavior of the enzyme.
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The line below this paragraph, {{ABSTRACT_PUBMED_11188693}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11188693 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11188693}}
==About this Structure==
==About this Structure==
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[[Category: Antiobitic resistance]]
[[Category: Antiobitic resistance]]
[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:37:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:06:24 2008''

Revision as of 21:06, 30 June 2008

Image:1e3u.png

Template:STRUCTURE 1e3u

MAD STRUCTURE OF OXA10 CLASS D BETA-LACTAMASE

Template:ABSTRACT PUBMED 11188693

About this Structure

1E3U is a Protein complex structure of sequences from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

Insights into class D beta-lactamases are revealed by the crystal structure of the OXA10 enzyme from Pseudomonas aeruginosa., Maveyraud L, Golemi D, Kotra LP, Tranier S, Vakulenko S, Mobashery S, Samama JP, Structure. 2000 Dec 15;8(12):1289-98. PMID:11188693

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