A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family

Pablo Perez-Garcia; Stefanie Kobus; Christoph G. W. Gertzen; Astrid Hoeppner; Nicholas Holzscheck; Christoph Heinrich Strunk; Harald Huber; Karl-Erich Jaeger; Holger Gohlke; Filip Kovacic; Sander H. J. Smits; Wolfgang R. Streit; Jennifer Chow

doi:10.1038/s42003-021-01671-8

Communications Biology (Jan 2021)

A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family

Pablo Perez-Garcia,
Stefanie Kobus,
Christoph G. W. Gertzen,
Astrid Hoeppner,
Nicholas Holzscheck,
Christoph Heinrich Strunk,
Harald Huber,
Karl-Erich Jaeger,
Holger Gohlke,
Filip Kovacic,
Sander H. J. Smits,
Wolfgang R. Streit,
Jennifer Chow

Affiliations

Pablo Perez-Garcia: Department of Microbiology and Biotechnology, University of Hamburg
Stefanie Kobus: Center for Structural Studies (CSS), Heinrich Heine University Düsseldorf
Christoph G. W. Gertzen: Center for Structural Studies (CSS), Heinrich Heine University Düsseldorf
Astrid Hoeppner: Center for Structural Studies (CSS), Heinrich Heine University Düsseldorf
Nicholas Holzscheck: Department of Microbiology and Biotechnology, University of Hamburg
Christoph Heinrich Strunk: Institute of Molecular Enzyme Technology (IMET), Heinrich Heine University Düsseldorf
Harald Huber: Institute for Microbiology and Archaeal Center, Regensburg University
Karl-Erich Jaeger: Institute of Molecular Enzyme Technology (IMET), Heinrich Heine University Düsseldorf
Holger Gohlke: John von Neumann Institute for Computing (NIC), Jülich Supercomputing Centre (JSC) & Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich GmbH
Filip Kovacic: Institute of Molecular Enzyme Technology (IMET), Heinrich Heine University Düsseldorf
Sander H. J. Smits: Center for Structural Studies (CSS), Heinrich Heine University Düsseldorf
Wolfgang R. Streit: Department of Microbiology and Biotechnology, University of Hamburg
Jennifer Chow: Department of Microbiology and Biotechnology, University of Hamburg

DOI: https://doi.org/10.1038/s42003-021-01671-8
Journal volume & issue: Vol. 4, no. 1
pp. 1 – 12

Abstract

Read online

The structure of Igni18, ancient enzyme from the Crenarchaean species Ignicoccus hospitalis, is solved and characterized by Pérez-García, Chow and colleagues. This structure provides insight as to the evolution of metallo-beta-lactamases and their functions.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

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