Ontology highlight
ABSTRACT:
SUBMITTER: Kato Y
PROVIDER: S-EPMC7599082 | biostudies-literature | 2020
REPOSITORIES: biostudies-literature
Kato Yoshiki Y Takahashi Masayuki M Seki Mineaki M Nashimoto Masayuki M Shimizu-Ibuka Akiko A
PloS one 20201030 10
Metallo-β-lactamases (MBLs) hydrolyze a wide range of β-lactam antibiotics. While all MBLs share a common αβ/βα-fold, there are many other proteins with the same folding pattern that exhibit different enzymatic activities. These enzymes, together with MBLs, form the MBL superfamily. Thermotoga maritima tRNase Z, a tRNA 3' processing endoribonuclease of MBL-superfamily, and IMP-1, a clinically isolated MBL, showed a striking similarity in tertiary structure, despite low sequence homology. IMP-1 h ...[more]