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Structure-based phylogeny of the metallo-beta-lactamases
Gianpiero Garau1, Anne Marie Di Guilmi, Barry G Hall
1Laboratoire de Cristallographie Macromoléulaire, Institut de Biologie Structural Jean-Pierre Ebel, CEA-CNRS-UJF, Grenoble, France.
Antimicrobial Agents and Chemotherapy
|June 28, 2005
Summary
Metallo-beta-lactamases, despite lacking sequence homology, share structural similarities. Phylogenetic analysis reveals their ancient origins across diverse life forms, suggesting a deep evolutionary history for this enzyme family.
Area of Science:
- Biochemistry
- Structural Biology
- Evolutionary Biology
Background:
- Metallo-beta-lactamases (MBLs) are crucial enzymes with two main groups: Ambler class B subgroups B1/B2 and B3.
- These groups exhibit no sequence homology but share detectable protein structure homology.
Purpose of the Study:
- To investigate the evolutionary relationships and origins of metallo-beta-lactamases.
- To construct a phylogenetic tree of MBLs and related proteins.
Main Methods:
- Utilized the Multiple Structure Alignment Program (MAPS) to align protein structures.
- Aligned eight metallo-beta-lactamases and five structurally homologous proteins.
- Constructed a phylogenetic tree based on the structural alignment.
Main Results:
- Established structural homology between distantly related MBL groups.
- The phylogenetic tree included genes from Eubacteria, Archaebacteria, and Eukaryota.
- Demonstrated significant evolutionary divergence within the MBL family.
Conclusions:
- Metallo-beta-lactamase family has a very ancient origin.
- Protein structure provides a more conserved evolutionary marker than sequence for MBLs.
- The findings highlight the deep evolutionary roots of MBLs across prokaryotic and eukaryotic domains.
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