1H, 15N, 13C resonance assignments for Saccharomyces cerevisiae Rad23 UBL domain

被引：1

作者：

Chen, Xiang ^{[1
]}

Walters, Kylie J. ^{[1
]}

机构：

[1] NCI, Prot Proc Sect, Struct Biophys Lab, Ctr Canc Res, Frederick, MD 21702 USA

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2016年 / 10卷 / 02期

关键词：

Ubiquitin-proteasome pathway; UV excision repair protein Rad23; Ubiquitin-like domain; NMR; UBIQUITIN-LIKE DOMAINS; REPAIR PROTEIN HHR23A; PROTEASOME; S5A; SUBUNIT; BINDING; DNA; RECEPTOR; RPN1; IDENTIFICATION;

D O I：

10.1007/s12104-016-9686-7

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Rad23 functions in nucleotide excision repair and proteasome-mediated protein degradation. It has four distinct structural domains that are connected by flexible linker regions, including an N-terminal ubiquitin-like (UBL) domain that binds proteasomes. We report in this NMR study the H-1, N-15 and C-13 resonance assignments for the backbone and side chain atoms of the Rad23 UBL domain (Rad23(UBL)) with BioMagResBank accession number 25825. We find that a Rad23 proline amino acid (P20) located in a loop undergoes isomerization. The secondary structural elements predicted from the NMR data fit well to that of the Rad23(UBL) when complexed with E4 ubiquitin ligase Ufd2, as reported in a crystallographic structure. These complete assignments can be used to study the protein dynamics of the Rad23(UBL) and its interaction of with other ubiquitin receptors or proteasome subunits.

引用

页码：291 / 295

页数：5

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