PDBsum entry 2gj2

Metal binding protein

PDB id: 2gj2

Contents

Protein chains

79 a.a. *

Metals

_CD ×8

Waters ×125

* Residue conservation analysis

PDB id:

2gj2

Name:

Metal binding protein

Title:

Crystal structure of vp9 from white spot syndrome virus

Structure:

Wsv230. Chain: a, b, c, d. Synonym: vp9. Engineered: yes

Source:

Shrimp white spot syndrome virus. Organism_taxid: 92652. Gene: wsv230. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.35Å R-factor: 0.225 R-free: 0.275

Authors:

Y.Liu,J.L.Wu,J.X.Song,J.Sivaraman,C.L.Hew

Key ref:

Y.Liu et al. (2006). Identification of a novel nonstructural protein, VP9, from white spot syndrome virus: its structure reveals a ferredoxin fold with specific metal binding sites. J Virol, 80, 10419-10427. PubMed id: 16956937

Date:

30-Mar-06 Release date: 19-Sep-06

Protein chains

Q91LD0  (Q91LD0_9VIRU) -  ICP11/P9 from White spot syndrome virus

Seq: 82 a.a.

Struc: 79 a.a.

Enzyme reactions

• Enzyme class: E.C.?

J Virol 80:10419-10427 (2006)

PubMed id: 16956937

Identification of a novel nonstructural protein, VP9, from white spot syndrome virus: its structure reveals a ferredoxin fold with specific metal binding sites.

Y.Liu, J.Wu, J.Song, J.Sivaraman, C.L.Hew.

ABSTRACT

White spot syndrome virus (WSSV) is a major pathogen in shrimp aquaculture. VP9, a full-length protein of WSSV, encoded by open reading frame wsv230, was identified for the first time in the infected Penaeus monodon shrimp tissues, gill, and stomach as a novel, nonstructural protein by Western blotting, mass spectrometry, and immunoelectron microscopy. Real-time reverse transcription-PCR demonstrated that the transcription of VP9 started from the early to the late stage of WSSV infection as a major mRNA species. The structure of full-length VP9 was determined by both X-ray and nuclear magnetic resonance (NMR) techniques. It is the first structure to be reported for WSSV proteins. The crystal structure of VP9 revealed a ferredoxin fold with divalent metal ion binding sites. Cadmium sulfate was found to be essential for crystallization. The Cd2+ ions were bound between the monomer interfaces of the homodimer. Various divalent metal ions have been titrated against VP9, and their interactions were analyzed using NMR spectroscopy. The titration data indicated that VP9 binds with both Zn2+ and Cd2+. VP9 adopts a similar fold as the DNA binding domain of the papillomavirus E2 protein. Based on our present investigations, we hypothesize that VP9 might be involved in the transcriptional regulation of WSSV, a function similar to that of the E2 protein during papillomavirus infection of the host cells.