Structure of theReston ebolavirusVP30 C-terminal domain

The ebolaviruses can cause severe hemorrhagic fever. Essential to the ebolavirus life cycle is the protein VP30, which serves as a transcriptional cofactor. Here, the crystal structure of the C-terminal, NP-binding domain of VP30 fromReston ebolavirusis presented. Reston VP30 and Ebola VP30 both form homodimers, but the dimeric interfaces are rotated relative to each other, suggesting subtle inherent differences or flexibility in the dimeric interface.

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Crystal structure of the N-terminal domain of VqsR fromPseudomonas aeruginosaat 2.1 Å resolution

Acta Crystallographica Section F Structural Biology Communications ◽

10.1107/s2053230x17009025 ◽

2017 ◽

Vol 73 (7) ◽

pp. 431-436

Author(s):

Qing He ◽

Kang Wang ◽

Tiantian Su ◽

Feng Wang ◽

Lichuan Gu ◽

...

Keyword(s):

Crystal Structure ◽

Sequence Similarity ◽

Transcriptional Regulator ◽

Binding Domain ◽

Structural Comparison ◽

Homoserine Lactones ◽

Terminal Domain ◽

C Terminus ◽

Common Motif ◽

The Common

VqsR is a quorum-sensing (QS) transcriptional regulator which controls QS systems (las,rhlandpqs) by directly downregulating the expression ofqscRinPseudomonas aeruginosa. As a member of the LuxR family of proteins, VqsR shares the common motif of a helix–turn–helix (HTH)-type DNA-binding domain at the C-terminus, while the function of its N-terminal domain remains obscure. Here, the crystal structure of the N-terminal domain of VqsR (VqsR-N; residues 1–193) was determined at a resolution of 2.1 Å. The structure is folded into a regular α–β–α sandwich topology, which is similar to the ligand-binding domain (LBD) of the LuxR-type QS receptors. Although their sequence similarity is very low, structural comparison reveals that VqsR-N has a conserved enclosed cavity which could recognize acyl-homoserine lactones (AHLs) as in other LuxR-type AHL receptors. The structure suggests that VqsR could be a potential AHL receptor.

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Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites

10.1101/2020.03.06.977876 ◽

2020 ◽

Cited By ~ 16

Author(s):

Sisi Kang ◽

Mei Yang ◽

Zhongsi Hong ◽

Liping Zhang ◽

Zhaoxia Huang ◽

...

Keyword(s):

Crystal Structure ◽

Nucleocapsid Protein ◽

Rna Binding ◽

Structural Information ◽

Antiviral Drug ◽

Binding Domain ◽

Binding Studies ◽

Terminal Domain ◽

Rna Binding Domain

AbstractThe outbreak of coronavirus disease (COVID-19) in China caused by SARS-CoV-2 virus continually lead to worldwide human infections and deaths. It is currently no specific viral protein targeted therapeutics yet. Viral nucleocapsid protein is a potential antiviral drug target, serving multiple critical functions during the viral life cycle. However, the structural information of SARS-CoV-2 nucleocapsid protein is yet to be clear. Herein, we have determined the 2.7 Å crystal structure of the N-terminal RNA binding domain of SARS-CoV-2 nucleocapsid protein. Although overall structure is similar with other reported coronavirus nucleocapsid protein N-terminal domain, the surface electrostatic potential characteristics between them are distinct. Further comparison with mild virus type HCoV-OC43 equivalent domain demonstrates a unique potential RNA binding pocket alongside the β-sheet core. Complemented by in vitro binding studies, our data provide several atomic resolution features of SARS-CoV-2 nucleocapsid protein N-terminal domain, guiding the design of novel antiviral agents specific targeting to SARS-CoV-2.

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Crystal Structure of the Oligomeric Form of Lassa Virus Matrix Protein Z

Journal of Virology ◽

10.1128/jvi.02896-15 ◽

2016 ◽

Vol 90 (9) ◽

pp. 4556-4562 ◽

Cited By ~ 14

Author(s):

Kathryn M. Hastie ◽

Michelle Zandonatti ◽

Tong Liu ◽

Sheng Li ◽

Virgil L. Woods ◽

...

Keyword(s):

Crystal Structure ◽

Life Cycle ◽

Matrix Protein ◽

Hemorrhagic Fever ◽

Viral Life Cycle ◽

Lassa Virus ◽

Protein Z ◽

Basic Center ◽

Oligomeric Form ◽

Oligomeric Forms

ABSTRACTThe arenavirus matrix protein Z is highly multifunctional and occurs in both monomeric and oligomeric forms. The crystal structure of a dodecamer of Z from Lassa virus, presented here, illustrates a ring-like structure with a highly basic center. Mutagenesis demonstrates that the dimeric interface within the dodecamer and a Lys-Trp-Lys triad at the center of the ring are important for oligomerization. This structure provides an additional template to explore the many functions of Z.IMPORTANCEThe arenavirus Lassa virus causes hundreds of thousands of infections each year, many of which develop into fatal hemorrhagic fever. The arenavirus matrix protein Z is multifunctional, with at least four distinct roles. Z exists in both monomeric and oligomeric forms, each of which likely serves a specific function in the viral life cycle. Here we present the dodecameric form of Lassa virus Z and demonstrate that Z forms a “wreath” with a highly basic center. This structure and that of monomeric Z now provide a pair of critical templates by which the multiple roles of Z in the viral life cycle may be interpreted.

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Crystal Structure of Marburg Virus VP40 Reveals a Broad, Basic Patch for Matrix Assembly and a Requirement of the N-Terminal Domain for Immunosuppression

Journal of Virology ◽

10.1128/jvi.01597-15 ◽

2015 ◽

Vol 90 (4) ◽

pp. 1839-1848 ◽

Cited By ~ 23

Author(s):

Shun-ichiro Oda ◽

Takeshi Noda ◽

Kaveesha J. Wijesinghe ◽

Peter Halfmann ◽

Zachary A. Bornholdt ◽

...

Keyword(s):

Crystal Structure ◽

Matrix Protein ◽

Ebola Virus ◽

Virus Assembly ◽

Hemorrhagic Fever ◽

Marburg Virus ◽

Molecular Structures ◽

Matrix Assembly ◽

Terminal Domain ◽

Terminal Domains

ABSTRACTMarburg virus (MARV), a member of the filovirus family, causes severe hemorrhagic fever with up to 90% lethality. MARV matrix protein VP40 is essential for assembly and release of newly copied viruses and also suppresses immune signaling in the infected cell. Here we report the crystal structure of MARV VP40. We found that MARV VP40 forms a dimer in solution, mediated by N-terminal domains, and that formation of this dimer is essential for budding of virus-like particles. We also found the N-terminal domain to be necessary and sufficient for immune antagonism. The C-terminal domains of MARV VP40 are dispensable for immunosuppression but are required for virus assembly. The C-terminal domains are only 16% identical to those of Ebola virus, differ in structure from those of Ebola virus, and form a distinct broad and flat cationic surface that likely interacts with the cell membrane during virus assembly.IMPORTANCEMarburg virus, a cousin of Ebola virus, causes severe hemorrhagic fever, with up to 90% lethality seen in recent outbreaks. Molecular structures and visual images of the proteins of Marburg virus are essential for the development of antiviral drugs. One key protein in the Marburg virus life cycle is VP40, which both assembles the virus and suppresses the immune system. Here we provide the molecular structure of Marburg virus VP40, illustrate differences from VP40 of Ebola virus, and reveal surfaces by which Marburg VP40 assembles progeny and suppresses immune function.

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