This title appears in the Scientific Report :
2021
Please use the identifier:
http://hdl.handle.net/2128/27113 in citations.
Please use the identifier: http://dx.doi.org/10.1038/s42003-021-01671-8 in citations.
A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family
A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family
The metallo-β-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 Å and could resemble a possible first...
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Personal Name(s): | Perez-Garcia, Pablo |
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Kobus, Stefanie / Gertzen, Christoph G. W. / Hoeppner, Astrid / Holzscheck, Nicholas / Strunk, Christoph Heinrich / Huber, Harald / Jaeger, Karl-Erich / Gohlke, Holger / Kovacic, Filip / Smits, Sander H. J. / Streit, Wolfgang R. / Chow, Jennifer (Corresponding author) | |
Contributing Institute: |
Institut für Molekulare Enzymtechnologie (HHUD); IMET Strukturbiochemie; IBI-7 Jülich Supercomputing Center; JSC John von Neumann - Institut für Computing; NIC |
Published in: | Communications biology, 4 (2021) 1, S. 132 |
Imprint: |
London
Springer Nature
2021
|
DOI: |
10.1038/s42003-021-01671-8 |
Document Type: |
Journal Article |
Research Program: |
Zentrum für strukturelle Studien Forschergruppe Gohlke Domain-Specific Simulation & Data Life Cycle Labs (SDLs) and Research Groups |
Link: |
OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1038/s42003-021-01671-8 in citations.
The metallo-β-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 Å and could resemble a possible first archetype of a multifunctional metallo-β-lactamase. Ancestral enzymes at the evolutionary origin are believed to be promiscuous all-rounders. Consistently, Igni18´s activity can be cofactor-dependently directed from β-lactamase to lactonase, lipase, phosphodiesterase, phosphotriesterase or phospholipase. Its core-domain is highly conserved within metallo-β-lactamases from Bacteria, Archaea and Eukarya and gives insights into evolution and function of enzymes from this superfamily. Structural alignments with diverse metallo-β-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. |