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1e25

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{{STRUCTURE_1e25| PDB=1e25 | SCENE= }}
{{STRUCTURE_1e25| PDB=1e25 | SCENE= }}
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'''THE HIGH RESOLUTION STRUCTURE OF PER-1 CLASS A BETA-LACTAMASE'''
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===THE HIGH RESOLUTION STRUCTURE OF PER-1 CLASS A BETA-LACTAMASE===
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==Overview==
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The treatment of infectious diseases by beta-lactam antibiotics is continuously challenged by the emergence and dissemination of new beta-lactamases. In most cases, the cephalosporinase activity of class A enzymes results from a few mutations in the TEM and SHV penicillinases. The PER-1 beta-lactamase was characterized as a class A enzyme displaying a cephalosporinase activity. This activity was, however, insensitive to the mutations of residues known to be critical for providing extended substrate profiles to TEM and SHV. The x-ray structure of the protein, solved at 1.9-A resolution, reveals that two of the most conserved features in class A beta-lactamases are not present in this enzyme: the fold of the Omega-loop and the cis conformation of the peptide bond between residues 166 and 167. The new fold of the Omega-loop and the insertion of four residues at the edge of strand S3 generate a broad cavity that may easily accommodate the bulky substituents of cephalosporin substrates. The trans conformation of the 166-167 bond is related to the presence of an aspartic acid at position 136. Selection of class A enzymes based on the occurrence of both Asp(136) and Asn(179) identifies a subgroup of enzymes with high sequence homology.
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(as it appears on PubMed at http://www.pubmed.gov), where 10825176 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10825176}}
==About this Structure==
==About this Structure==
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[[Category: Class a cephalosporinase]]
[[Category: Class a cephalosporinase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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Revision as of 21:01, 30 June 2008

Image:1e25.png

Template:STRUCTURE 1e25

THE HIGH RESOLUTION STRUCTURE OF PER-1 CLASS A BETA-LACTAMASE

Template:ABSTRACT PUBMED 10825176

About this Structure

1E25 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

The high resolution crystal structure for class A beta-lactamase PER-1 reveals the bases for its increase in breadth of activity., Tranier S, Bouthors AT, Maveyraud L, Guillet V, Sougakoff W, Samama JP, J Biol Chem. 2000 Sep 8;275(36):28075-82. PMID:10825176

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