2WYQ

THE CRYSTAL STRUCTURE OF THE UBIQUITIN-LIKE (UBL) DOMAIN OF HHR23A (HUMAN HOMOLOGUE A OF RAD23)

2WYQ の概要

• エントリーDOI: 10.2210/pdb2wyq/pdb
• 関連するPDBエントリー: 1DV0 1F4I 1IFY 1OQY 1P98 1P9D 1QZE 1TP4
• 分子名称: UV EXCISION REPAIR PROTEIN RAD23 HOMOLOG A, SULFATE ION (3 entities in total)
• 機能のキーワード: dna binding protein, dna excision repair, proteasomal degradation, polyubiquitin
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Nucleus: P54725
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9771.40

構造登録者

Chen, Y.W. (登録日: 2009-11-19, 公開日: 2010-11-10, 最終更新日: 2023-12-20)

主引用文献

Chen, Y.W.,Tajima, T.,Agrawal, S.
The Crystal Structure of the Ubiquitin-Like (Ubl) Domain of Human Homologue a of Rad23 (Hhr23A) Protein
Protein Eng.Des.Sel., 24:131-, 2011

PubMed Abstract: The human homologue of the yeast Rad23 protein, hHR23A, plays dual roles in DNA repair as well as in translocating polyubiquitinated proteins to the proteasome. We determined the three-dimensional structure of its ubiquitin-like (UbL) domain by X-ray crystallography. It has the same overall structure and fold characteristics as ubiquitin and other members of the UbL domain family, with overall root mean square deviations in Cα positions in the range of 1.0-1.3 Å. There are local differences in the α1-β3 loop where hHR23A UbL domain has three more residues constituting a bigger loop. Analysis of the crystal packing revealed a possible dimeric arrangement mediated by the three residues (Leu10, Ile49 and Met75) that are known to be critical for molecular interactions. In contrast to the overall well-defined structure, these three residues are either disordered or have multiple conformations, suggesting that conformation variability is an important property of the binding surface. The electrostatic potentials at the binding surface are conserved among the family, with the hHR23B domain being the most similar to this structure. The intra-molecular complexes formed by the UbL domain of hHR23A with its UbA1 or UbA2 domains was studied by comparative homology modelling, which suggests these two interactions are structurally similar and are mutually exclusive.

PubMed: 21047872
DOI: 10.1093/PROTEIN/GZQ084

実験手法

X-RAY DIFFRACTION (1.651 Å)