Article

Abstract

• Understanding how proteins adapt to function at high temperatures is important for deciphering the energetics that dictate protein stability and folding. While multiple principles important for thermostability have been identified, we lack a unified understanding of how internal protein structural and chemical environment determine qualitative or quantitative impact of evolutionary mutations. In this work we compare equivalent clusters of spatially neighboring residues between paired thermophilic and mesophilic homologues to evaluate adaptations under the selective pressure of high temperature. We find the residue clusters in thermophilic enzymes generally display improved atomic packing compared to mesophilic enzymes, in agreement with previous research. Unlike residue clusters from mesophilic enzymes, however, thermophilic residue clusters do not have significant cavities. In addition, anchor residues found in many clusters are highly conserved with respect to atomic packing between both thermophilic and mesophilic enzymes. Thus the improvements in atomic packing observed in thermophilic homologues are not derived from these anchor residues but from neighboring positions, which may serve to expand optimized protein core regions.

Creator

• Bomble, Yannick J
• Yin, Hang
• Sammond, Deanne W
• Himmel, Michael E
• Kastelowitz, Noah
• Crowley, Michael F

Date Issued

• 2016-01-01

Academic Affiliation

• Chemical and Biological Engineering

Journal Title

• PLoS One

Journal Issue/Number

• 1

Journal Volume

• 11

File Extent

• 0145848-0145848

Subject

• Tertiary
• Hot Temperature
• Protein Stability
• Archaea
• Fungi
• Aminopeptidases
• Archaeal Proteins
• Protein Folding
• Malate Dehydrogenase
• Bacteria
• Molecular Sequence Data
• Molecular
• Secondary
• Amino Acid Sequence
• Protein Structure
• Fungal Proteins
• Models
• L-Lactate Dehydrogenase
• Amino Acids
• Cluster Analysis
• Bacterial Proteins

Last Modified

• 2019-12-05

Identifier

• PubMed ID: 26741367

Resource Type

• Article

Rights Statement

• In Copyright

DOI

•  https://doi.org/10.1371/journal.pone.0145848

ISSN

• 1932-6203

Language

• English [eng]

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