Crystal structure of the herpesvirus inner tegument protein UL37 supports its essential role in control of viral trafficking.

ABSTRACT:

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In cells infected with herpesviruses, two capsid-associated, or inner tegument, proteins, UL37 and UL36, control cytosolic trafficking of capsids by as yet poorly understood mechanisms. Here, we report the crystal structure of the N-terminal half of UL37 from pseudorabies virus, an alphaherpesvirus closely related to herpes simplex viruses and varicella-zoster virus. The structure--the first for any alphaherpesvirus inner tegument protein--reveals an elongated molecule of a complex architecture rich in helical bundles. To explore the function of the UL37 N terminus, we used the three-dimensional framework provided by the structure in combination with evolutionary trace analysis to pinpoint several surface-exposed regions of potential functional importance and test their

SUBMITTER: Pitts JD 

PROVIDER: S-EPMC4019128 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature