PDBsum entry 5hlj

Viral protein

PDB id: 5hlj

Contents

Protein chain

169 a.a.

Waters ×54

PDB id:

5hlj

Name:

Viral protein

Title:

Crystal structure of major envelope protein vp24 from white spot syndrome virus

Structure:

Vp24. Chain: a. Fragment: unp residues 30-208. Engineered: yes

Source:

White spot syndrome virus. Organism_taxid: 342409. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.41Å R-factor: 0.173 R-free: 0.193

Authors:

L.F.Sun,Y.T.Su,Y.H.Zhao,Z.Q.Fu,Y.K.Wu

Key ref:

L.Sun et al. (2016). Crystal Structure of Major Envelope Protein VP24 from White Spot Syndrome Virus. Sci Rep, 6, 32309. PubMed id: 27572278

Date:

15-Jan-16 Release date: 14-Sep-16

Protein chain

Q80BF2  (Q80BF2_9VIRU) -  VP24 from White spot syndrome virus

Seq: 208 a.a.

Struc: 169 a.a.

Enzyme reactions

• Enzyme class: E.C.?

Sci Rep 6:32309 (2016)

PubMed id: 27572278

Crystal Structure of Major Envelope Protein VP24 from White Spot Syndrome Virus.

L.Sun, Y.Su, Y.Zhao, Z.Q.Fu, Y.Wu.

ABSTRACT

White spot syndrome virus (WSSV) is one of the major and most serious pathogen in the shrimp industry. As one of the most abundant envelope protein, VP24 acts as a core protein interacting with other structure proteins and plays an important role in virus assembly and infection. Here, we have presented the crystal structure of VP24 from WSSV. In the structure, VP24 consists of a nine-stranded β-barrel fold with mostly antiparallel β-strands, and the loops extending out the β-barrel at both N-terminus and C-terminus, which is distinct to those of the other two major envelope proteins VP28 and VP26. Structural comparison of VP24 with VP26 and VP28 reveals opposite electrostatic surface potential properties of them. These structural differences could provide insight into their differential functional mechanisms and roles for virus assembly and infection. Moreover, the structure reveals a trimeric assembly, suggesting a likely natural conformation of VP24 in viral envelope. Therefore, in addition to confirming the evolutionary relationship among the three abundant envelope proteins of WSSV, our structural studies also facilitate a better understanding of the molecular mechanism underlying special roles of VP24 in WSSV assembly and infection.