PDBsum entry 1vzv

Serine protease

PDB id: 1vzv

Contents

Protein chain

211 a.a. *

* Residue conservation analysis

PDB id:

1vzv

Name:

Serine protease

Title:

Structure of varicella-zoster virus protease

Structure:

Varicella-zoster virus protease. Chain: a. Fragment: residues 10 - 236. Synonym: assemblin. Engineered: yes. Mutation: yes

Source:

Human herpesvirus 3. Varicella-zoster virus. Organism_taxid: 10335. Strain: acyclovir-resistant strain 40a2. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PQS)

Resolution:

3.00Å R-factor: 0.223

Authors:

X.Qiu,C.A.Jason,J.S.Culp,S.B.Richardson,C.Debouck,W.W.Smith, S.S.Abdel-Meguid

Key ref:

X.Qiu et al. (1997). Crystal structure of varicella-zoster virus protease. Proc Natl Acad Sci U S A, 94, 2874-2879. PubMed id: 9096314 DOI: 10.1073/pnas.94.7.2874

Date:

10-Feb-97 Release date: 16-Sep-98

Protein chain

P09286  (SCAF_VZVD) -  Capsid scaffolding protein from Varicella-zoster virus (strain Dumas)

Seq: 605 a.a.

Struc: 211 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.21.97 - assemblin.
• Reaction: Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.

DOI no: 10.1073/pnas.94.7.2874

Proc Natl Acad Sci U S A 94:2874-2879 (1997)

PubMed id: 9096314

Crystal structure of varicella-zoster virus protease.

X.Qiu, C.A.Janson, J.S.Culp, S.B.Richardson, C.Debouck, W.W.Smith, S.S.Abdel-Meguid.

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.

Selected figure(s)

Figure 4.
Fig. 4. The catalytic residues (A) in the omit F[o] F[c] map contoured at 3 . (B) VZV protease (red) compared with CMV (blue) and trypsin (yellow). Dashed lines connects the catalytic triad of the VZV protease. Only CMV numbering is used.

Figure 5.
Fig. 5. Molecular surface of the VZV protease looking into the postulated substrate binding groove. The surface is color-coded by electrostatic potentials (blue for positive and red for negative) calculated with the program GRASP (28). Modeled is the Ala-Ser cleavage site. The red arrow indicates the position of the scissile^ bond.

Figures were selected by an automated process.