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A structural basis for processivity.

W A Breyer¹, B W Matthews

¹Institute of Molecular Biology, Howard Hughes Medical Institute and Department of Physics, University of Oregon, Eugene, Oregon 97403-1229, USA.

Protein Science : a Publication of the Protein Society

|August 22, 2001

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Processive enzymes, which remain attached to substrates for thousands of catalytic rounds, are categorized by substrate enclosure. Complete enclosure, often topological, explains processivity, while partial enclosure relies on large interaction surfaces.

Area of Science:

Biochemistry
Structural Biology
Enzymology

Background:

Processive enzymes remain bound to polymeric substrates for extended catalytic cycles.
Enzyme structure dictates substrate interaction and processivity mechanisms.
Recent structural studies reveal diverse strategies for enzyme-substrate engagement.

Purpose of the Study:

To categorize enzyme structures based on substrate enclosure.
To elucidate the structural basis of enzyme processivity.
To understand how enzymes maintain prolonged interaction with polymeric substrates.

Main Methods:

Structural determination of processive enzymes.
Comparative analysis of enzyme structures and their substrate interaction modes.

Related Experiment Videos

Correlation of structural features with observed processivity.

Main Results:

Enzymes are classified into two groups: partial and complete substrate enclosure.
Complete enclosure, achieved via asymmetric or toroidal structures, leads to topological linkage and explains processivity.
Partial enclosure relies on large interaction surfaces for moderate affinity binding across multiple sites, facilitating sliding.

Conclusions:

Enzyme processivity is structurally determined by the degree of substrate enclosure.
Complete enclosure provides a direct mechanism for processivity through topological restraint.
Partial enclosure utilizes extensive surface interactions to maintain enzyme-substrate association and facilitate sliding.