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Evolutionary link between glycogen phosphorylase and a DNA modifying enzyme

L Holm¹, C Sander

¹EMBL, Heidelberg, Germany.

The EMBO Journal

|April 3, 1995

Summary

Structural similarities were found between DNA modifying beta-glucosyltransferase and metabolic glycogen phosphorylase enzymes. This suggests a common evolutionary origin for these glucosyltransferases.

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Area of Science:

Biochemistry
Structural Biology
Evolutionary Biology

Background:

Glucosyltransferases are enzymes involved in diverse biochemical pathways.
Bacteriophage T4 beta-glucosyltransferase modifies DNA, while glycogen phosphorylase is a metabolic enzyme.

Purpose of the Study:

To investigate structural similarities between beta-glucosyltransferase and glycogen phosphorylase.
To explore the evolutionary and functional implications of these similarities.

Main Methods:

Structural alignment of beta-glucosyltransferase and glycogen phosphorylase.
Analysis of domain orientation, connecting helices, and root-mean-square deviation.
Comparison of substrate binding and functional analogies.

Main Results:

Beta-glucosyltransferase's structure is topographically equivalent to glycogen phosphorylase's catalytic core.
A 3.4 A root-mean-square deviation was observed for 256 C alpha atoms.
Similar interdomain rotations were noted during substrate binding and state transitions.

Conclusions:

The findings reveal unexpected structural conservation in glucosyltransferases across different pathways.
This suggests a common evolutionary ancestor for these enzymes.
The study anticipates the identification of more structurally related glucosyltransferases.

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