دورية أكاديمية
أعرض في EDS

HSV-1 ICP0 dimer domain adopts a novel β-barrel fold.

التفاصيل البيبلوغرافية
العنوان: HSV-1 ICP0 dimer domain adopts a novel β-barrel fold.
المؤلفون: McCloskey E; Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas, USA., Kashipathy M; Protein Structure and X-Ray Crystallography Laboratory, University of Kansas, Lawrence, Kansas, USA., Cooper A; Protein Production Group, University of Kansas, Lawrence, Kansas, USA., Gao P; Protein Production Group, University of Kansas, Lawrence, Kansas, USA., Johnson DK; Chemical Computational Biology Core, University of Kansas, Lawrence, Kansas, USA., Battaile KP; NYX, New York Structural Biology Center, Upton, New York, USA., Lovell S; Protein Structure and X-Ray Crystallography Laboratory, University of Kansas, Lawrence, Kansas, USA., Davido DJ; Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas, USA.
المصدر: Proteins [Proteins] 2024 Jul; Vol. 92 (7), pp. 830-841. Date of Electronic Publication: 2024 Feb 19.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Wiley-Liss Country of Publication: United States NLM ID: 8700181 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1097-0134 (Electronic) Linking ISSN: 08873585 NLM ISO Abbreviation: Proteins Subsets: MEDLINE
أسماء مطبوعة: Publication: New York, NY : Wiley-Liss
Original Publication: New York : Alan R. Liss, c1986-
مواضيع طبية MeSH: Immediate-Early Proteins*/chemistry , Immediate-Early Proteins*/metabolism , Immediate-Early Proteins*/genetics , Herpesvirus 1, Human* , Ubiquitin-Protein Ligases*/chemistry , Ubiquitin-Protein Ligases*/metabolism , Protein Multimerization*, Crystallography, X-Ray ; Models, Molecular ; Humans ; Protein Domains ; Protein Folding ; Amino Acid Sequence ; Protein Conformation, beta-Strand
مستخلص: Infected cell protein 0 (ICP0) is an immediate-early regulatory protein of herpes simplex virus 1 (HSV-1) that possesses E3 ubiquitin ligase activity. ICP0 transactivates viral genes, in part, through its C-terminal dimer domain (residues 555-767). Deletion of this dimer domain results in reduced viral gene expression, lytic infection, and reactivation from latency. Since ICP0's dimer domain is associated with its transactivation activity and efficient viral replication, we wanted to determine the structure of this specific domain. The C-terminus of ICP0 was purified from bacteria and analyzed by X-ray crystallography to solve its structure. Each subunit or monomer in the ICP0 dimer is composed of nine β-strands and two α-helices. Interestingly, two adjacent β-strands from one monomer "reach" into the adjacent subunit during dimer formation, generating two β-barrel-like structures. Additionally, crystallographic analyses indicate a tetramer structure is formed from two β-strands of each dimer, creating a "stacking" of the β-barrels. The structural protein database searches indicate the fold or structure adopted by the ICP0 dimer is novel. The dimer is held together by an extensive network of hydrogen bonds. Computational analyses reveal that ICP0 can either form a dimer or bind to SUMO1 via its C-terminal SUMO-interacting motifs but not both. Understanding the structure of the dimer domain will provide insights into the activities of ICP0 and, ultimately, the HSV-1 life cycle.
(© 2024 Wiley Periodicals LLC.)
التعليقات: Update of: bioRxiv. 2024 Jan 16:2024.01.16.575752. doi: 10.1101/2024.01.16.575752. (PMID: 38293217)
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معلومات مُعتمدة: DE-AC02-06CH11357 U.S. Department of Energy; P20GM113117 United States NH NIH HHS; P20 GM113117 United States GM NIGMS NIH HHS; P30 GM110761 United States GM NIGMS NIH HHS; Industrial Macromolecular Crystallography Association Collaborative Access Team; T32 GM132061 United States GM NIGMS NIH HHS; T32GM132061 United States NH NIH HHS; NIGMS; University of Kansas; P30GM110761 United States NH NIH HHS
فهرسة مساهمة: Keywords: HSV‐1; ICP0; beta‐barrel; crystal structure; dimerization; novel fold
المشرفين على المادة: 0 (Immediate-Early Proteins)
EC 2.3.2.27 (Vmw110 protein, Human herpesvirus 1)
EC 2.3.2.27 (Ubiquitin-Protein Ligases)
تواريخ الأحداث: Date Created: 20240219 Date Completed: 20240603 Latest Revision: 20240614
رمز التحديث: 20240615
مُعرف محوري في PubMed: PMC11147711
DOI: 10.1002/prot.26673
PMID: 38372168
قاعدة البيانات: MEDLINE
الوصف
تدمد:1097-0134
DOI:10.1002/prot.26673