1E25
The high resolution structure of PER-1 class A beta-lactamase
Summary for 1E25
| Entry DOI | 10.2210/pdb1e25/pdb |
| Descriptor | EXTENDED-SPECTRUM BETA-LACTAMASE PER-1, SULFATE ION (3 entities in total) |
| Functional Keywords | hydrolase, antibiotic resistance, class a cephalosporinase |
| Biological source | PSEUDOMONAS AERUGINOSA |
| Total number of polymer chains | 1 |
| Total formula weight | 31041.59 |
| Authors | Tranier, S.,Bouthors, A.T.,Maveyraud, L.,Guillet, V.,Sougakoff, W.,Samama, J.P. (deposition date: 2000-05-17, release date: 2000-11-06, Last modification date: 2024-05-08) |
| Primary citation | Tranier, S.,Bouthors, A.T.,Maveyraud, L.,Guillet, V.,Sougakoff, W.,Samama, J.P. The High Resolution Crystal Structure for Class a Beta-Lactamase Per-1 Reveals the Bases for its Increase in Breadth of Activity J.Biol.Chem., 275:28075-, 2000 Cited by PubMed Abstract: 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. PubMed: 10825176DOI: 10.1074/JBC.M003802200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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