1AT3

HERPES SIMPLEX VIRUS TYPE II PROTEASE

Summary for 1AT3

• Entry DOI: 10.2210/pdb1at3/pdb
• Descriptor: HERPES SIMPLEX VIRUS TYPE II PROTEASE, DIISOPROPYL PHOSPHONATE (3 entities in total)
• Functional Keywords: serine protease, viral protease, hsv2 protease
• Biological source: Human herpesvirus 2 (Herpes simplex virus type 2)
• Cellular location: Capsid scaffolding protein: Host cytoplasm . Assembly protein: Host nucleus . Assemblin: Host nucleus : Q69527
• Total number of polymer chains: 2
• Total formula weight: 54444.27

Authors

Hoog, S.,Smith, W.W.,Qiu, X.,Abdel-Meguid, S.S. (deposition date: 1997-08-16, release date: 1998-10-14, Last modification date: 2024-10-16)

Primary citation

Hoog, S.S.,Smith, W.W.,Qiu, X.,Janson, C.A.,Hellmig, B.,McQueney, M.S.,O'Donnell, K.,O'Shannessy, D.,DiLella, A.G.,Debouck, C.,Abdel-Meguid, S.S.
Active site cavity of herpesvirus proteases revealed by the crystal structure of herpes simplex virus protease/inhibitor complex.
Biochemistry, 36:14023-14029, 1997

PubMed Abstract: Human herpes simplex virus type 1 (HSV-1) and type 2 (HSV-2) are responsible for herpes labialis (cold sores) and genital herpes, respectively. They encode a serine protease that is required for viral replication, and represent a viable target for therapeutic intervention. Here, we report the crystal structures of HSV-1 and HSV-2 proteases, the latter in the presence and absence of the covalently bound transition state analog inhibitor diisopropyl phosphate (DIP). The HSV-1 and HSV-2 protease structures show a fold that is neither like chymotrypsin nor like subtilisin, and has been seen only in the recently determined cytomegalovirus (CMV) and varicella-zoster virus (VZV) protease structures. HSV-1 and HSV-2 proteases share high sequence homology and have almost identical three-dimensional structures. However, structural differences are observed with the less homologous CMV protease, offering a structural basis for herpes virus protease ligand specificity. The bound inhibitor identifies the oxyanion hole of these enzymes and defines the active site cavity.

PubMed: 9369473
DOI: 10.1021/bi9712697

Experimental method

X-RAY DIFFRACTION (2.5 Å)