Perez-Garcia, Pablo and Kobus, Stefanie and Gertzen, Christoph G. W. and Hoeppner, Astrid and Holzscheck, Nicholas and Strunk, Christoph Heinrich and Huber, Harald and Jaeger, Karl-Erich and Gohlke, Holger and Kovacic, Filip and Smits, Sander H. J. and Streit, Wolfgang R. and Chow, Jennifer (2021) A promiscuous ancestral enzyme ' s structure unveils protein variable regions of the highly diverse metallo-beta-lactamase family. COMMUNICATIONS BIOLOGY, 4 (1): 132. ISSN , 2399-3642
Full text not available from this repository. (Request a copy)Abstract
The metallo-beta -lactamase fold is an ancient protein structure present in numerous enzyme families responsible for diverse biological processes. The crystal structure of the hyperthermostable crenarchaeal enzyme Igni18 from Ignicoccus hospitalis was solved at 2.3 angstrom and could resemble a possible first archetype of a multifunctional metallo-beta -lactamase. Ancestral enzymes at the evolutionary origin are believed to be promiscuous all-rounders. Consistently, Igni18s activity can be cofactor-dependently directed from beta -lactamase to lactonase, lipase, phosphodiesterase, phosphotriesterase or phospholipase. Its core-domain is highly conserved within metallo-beta -lactamases from Bacteria, Archaea and Eukarya and gives insights into evolution and function of enzymes from this superfamily. Structural alignments with diverse metallo-beta -lactamase-fold-containing enzymes allowed the identification of Protein Variable Regions accounting for modulation of activity, specificity and oligomerization patterns. Docking of different substrates within the active sites revealed the basis for the crucial cofactor dependency of this enzyme superfamily. The structure of Igni18, ancient enzyme from the Crenarchaean species Ignicoccus hospitalis, is solved and characterized by Perez-Garcia, Chow and colleagues. This structure provides insight as to the evolution of metallo-beta-lactamases and their functions.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PARTICLE MESH EWALD; IGNICOCCUS-HOSPITALIS; MOLECULAR-DYNAMICS; PHOSPHOLIPASE-D; ORIGIN; SPECIFICITY; PARAMETERS; PREDICTION; HYDROLASE; MECHANISM; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 23 Sep 2022 05:15 |
| Last Modified: | 23 Sep 2022 05:15 |
| URI: | https://pred.uni-regensburg.de/id/eprint/47890 |
Actions (login required)
 |
View Item |
