1E25

The high resolution structure of PER-1 class A beta-lactamase

1E25 の概要

• エントリーDOI: 10.2210/pdb1e25/pdb
• 分子名称: EXTENDED-SPECTRUM BETA-LACTAMASE PER-1, SULFATE ION (3 entities in total)
• 機能のキーワード: hydrolase, antibiotic resistance, class a cephalosporinase
• 由来する生物種: PSEUDOMONAS AERUGINOSA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31041.59

構造登録者

Tranier, S.,Bouthors, A.T.,Maveyraud, L.,Guillet, V.,Sougakoff, W.,Samama, J.P. (登録日: 2000-05-17, 公開日: 2000-11-06, 最終更新日: 2024-05-08)

主引用文献

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

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: 10825176
DOI: 10.1074/JBC.M003802200

実験手法

X-RAY DIFFRACTION (1.9 Å)