Journal of Molecular Evolution

, Volume 57, Issue 3, pp 255–260

Structure-Based Phylogenies of the Serine β-Lactamases

Article

DOI: 10.1007/s00239-003-2473-y

Cite this article as:
Hall, B.G. & Barlow, M. J Mol Evol (2003) 57: 255. doi:10.1007/s00239-003-2473-y
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Abstract

The serine β-lactamases present a special problem for phylogenetics because they have diverged so much that they fall into three classes that share no detectable sequence homology among themselves. Here we offer a solution to the problem in the form of two phylogenies that are based on a protein structure alignment. In the first, structural alignments were used as a guide for aligning amino acid sequences and in the second, the average root mean square distances between the alpha carbons of the proteins were used to create a pairwise distance matrix from which a neighbor-joining phylogeny was created. From those phylogenies, we show that the Class A and Class D β-lactamases are sister taxa and that the divergence of the Class C β-lactamases predated the divergence of the Class A and Class D β-lactamases.

Keywords

Protein structureBayesian phylogenyβ-Lactamases

Copyright information

© Springer-Verlag New York Inc. 2003

Authors and Affiliations

  1. 1.Biology Department, Hutchison HallUniversity of Rochester, Rochester, NY 14627-0211USA