1e25: Difference between revisions

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[[Image:1e25.gif|left|200px]]
{{Seed}}
[[Image:1e25.png|left|200px]]


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{{STRUCTURE_1e25|  PDB=1e25  |  SCENE=  }}  
{{STRUCTURE_1e25|  PDB=1e25  |  SCENE=  }}  


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




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_10825176}}, adds the Publication Abstract to the page
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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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