Double‐stranded DNA bacteriophage prohead protease is homologous to herpesvirus protease

Double‐stranded DNA bacteriophage prohead protease is homologous to herpesvirus protease Double‐stranded DNA bacteriophages and herpesviruses assemble their heads in a similar fashion; a pre‐formed precursor called a prohead or procapsid undergoes a conformational transition to give rise to a mature head or capsid. A virus‐encoded prohead or procapsid protease is often required in this maturation process. Through computational analysis, we infer homology between bacteriophage prohead proteases (MEROPS families U9 and U35) and herpesvirus protease (MEROPS family S21), and unify them into a procapsid protease superfamily. We also extend this superfamily to include an uncharacterized cluster of orthologs (COG3566) and many other phage or bacteria‐encoded hypothetical proteins. On the basis of this homology and the herpesvirus protease structure and catalytic mechanism, we predict that bacteriophage prohead proteases adopt the herpesvirus protease fold and exploit a conserved Ser and His residue pair in catalysis. Our study provides further support for the proposed evolutionary link between dsDNA bacteriophages and herpesviruses. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Protein Science Wiley

Double‐stranded DNA bacteriophage prohead protease is homologous to herpesvirus protease

Protein Science, Volume 13 (8) – Aug 1, 2004

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Publisher
Wiley
Copyright
Copyright © 2004 The Protein Society
ISSN
0961-8368
eISSN
1469-896X
DOI
10.1110/ps.04726004
Publisher site
See Article on Publisher Site

Abstract

Double‐stranded DNA bacteriophages and herpesviruses assemble their heads in a similar fashion; a pre‐formed precursor called a prohead or procapsid undergoes a conformational transition to give rise to a mature head or capsid. A virus‐encoded prohead or procapsid protease is often required in this maturation process. Through computational analysis, we infer homology between bacteriophage prohead proteases (MEROPS families U9 and U35) and herpesvirus protease (MEROPS family S21), and unify them into a procapsid protease superfamily. We also extend this superfamily to include an uncharacterized cluster of orthologs (COG3566) and many other phage or bacteria‐encoded hypothetical proteins. On the basis of this homology and the herpesvirus protease structure and catalytic mechanism, we predict that bacteriophage prohead proteases adopt the herpesvirus protease fold and exploit a conserved Ser and His residue pair in catalysis. Our study provides further support for the proposed evolutionary link between dsDNA bacteriophages and herpesviruses.

Journal

Protein ScienceWiley

Published: Aug 1, 2004

References

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