6hrg
Structure of Igni18, a novel metallo hydrolase from the hyperthermophilic archaeon Ignicoccus hospitalis KIN4/IStructure of Igni18, a novel metallo hydrolase from the hyperthermophilic archaeon Ignicoccus hospitalis KIN4/I
Structural highlights
Publication Abstract from PubMedThe 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 A 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, Igni18 s 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. A promiscuous ancestral enzyme s structure unveils protein variable regions of the highly diverse metallo-beta-lactamase family.,Perez-Garcia P, Kobus S, Gertzen CGW, Hoeppner A, Holzscheck N, Strunk CH, Huber H, Jaeger KE, Gohlke H, Kovacic F, Smits SHJ, Streit WR, Chow J Commun Biol. 2021 Jan 29;4(1):132. doi: 10.1038/s42003-021-01671-8. PMID:33514861[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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