5DOC

Crystal structure of the Human Cytomegalovirus UL53 subunit of the NEC

5DOC の概要

• エントリーDOI: 10.2210/pdb5doc/pdb
• 関連するPDBエントリー: 5DOB 5DOE
• 分子名称: Virion egress protein UL31 homolog, ZINC ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: zinc finger, bergerat fold, conserved regions, dna binding protein
• 由来する生物種: Human cytomegalovirus (strain AD169) (HHV-5)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46629.78

構造登録者

Lye, M.F.,El Omari, K.,Filman, D.J.,Hogle, J.M. (登録日: 2015-09-11, 公開日: 2015-11-25, 最終更新日: 2024-03-06)

主引用文献

Lye, M.F.,Sharma, M.,El Omari, K.,Filman, D.J.,Schuermann, J.P.,Hogle, J.M.,Coen, D.M.
Unexpected features and mechanism of heterodimer formation of a herpesvirus nuclear egress complex.
Embo J., 34:2937-2952, 2015

PubMed Abstract: Herpesvirus nucleocapsids escape from the nucleus in a process orchestrated by a highly conserved, viral nuclear egress complex. In human cytomegalovirus, the complex consists of two proteins, UL50 and UL53. We solved structures of versions of UL53 and the complex by X-ray crystallography. The UL53 structures, determined at 1.93 and 3.0 Å resolution, contained unexpected features including a Bergerat fold resembling that found in certain nucleotide-binding proteins, and a Cys3His zinc finger. Substitutions of zinc-coordinating residues decreased UL50-UL53 co-localization in transfected cells, and, when incorporated into the HCMV genome, ablated viral replication. The structure of the complex, determined at 2.47 Å resolution, revealed a mechanism of heterodimerization in which UL50 clamps onto helices of UL53 like a vise. Substitutions of particular residues on the interaction interface disrupted UL50-UL53 co-localization in transfected cells and abolished virus production. The structures and the identification of contacts can be harnessed toward the rational design of novel and highly specific antiviral drugs and will aid in the detailed understanding of nuclear egress.

PubMed: 26511021
DOI: 10.15252/embj.201592651

実験手法

X-RAY DIFFRACTION (1.94 Å)