1VZV

STRUCTURE OF VARICELLA-ZOSTER VIRUS PROTEASE

Summary for 1VZV

• Entry DOI: 10.2210/pdb1vzv/pdb
• Descriptor: VARICELLA-ZOSTER VIRUS PROTEASE (1 entity in total)
• Functional Keywords: hydrolase, serine protease, viral protease, varicella-zoster virus, coat protein
• Biological source: Human herpesvirus 3 (Varicella-zoster virus)
• Cellular location: Protease precursor: Host cytoplasm. Assemblin: Host nucleus. Assembly protein: Host nucleus: P09286
• Total number of polymer chains: 1
• Total formula weight: 24654.53

Authors

Qiu, X.,Jason, C.A.,Culp, J.S.,Richardson, S.B.,Debouck, C.,Smith, W.W.,Abdel-Meguid, S.S. (deposition date: 1997-02-10, release date: 1998-09-16, Last modification date: 2024-02-14)

Primary citation

Qiu, X.,Janson, C.A.,Culp, J.S.,Richardson, S.B.,Debouck, C.,Smith, W.W.,Abdel-Meguid, S.S.
Crystal structure of varicella-zoster virus protease.
Proc.Natl.Acad.Sci.USA, 94:2874-2879, 1997

PubMed Abstract: Varicella-zoster virus (VZV), an alpha-herpes virus, is the causative agent of chickenpox, shingles, and postherpetic neuralgia. The three-dimensional crystal structure of the serine protease from VZV has been determined at 3.0-A resolution. The VZV protease is essential for the life cycle of the virus and is a potential target for therapeutic intervention. The structure reveals an overall fold that is similar to that recently reported for the serine protease from cytomegalovirus (CMV), a herpes virus of the beta subfamily. The VZV protease structure provides further evidence to support the finding that herpes virus proteases have a fold and active site distinct from other serine proteases. The VZV protease catalytic triad consists of a serine and two histidines. The distal histidine is proposed to properly orient the proximal histidine. The identification of an alpha-helical segment in the VZV protease that was mostly disordered in the CMV protease provides a better definition of the postulated active site cavity and reveals an elastase-like S' region. Structural differences between the VZV and CMV proteases also suggest potential differences in their oligomerization states.

PubMed: 9096314
DOI: 10.1073/pnas.94.7.2874

Experimental method

X-RAY DIFFRACTION (3 Å)