6JQV

Crystal structure of Arabidopsis thaliana NRP2

6JQV の概要

• エントリーDOI: 10.2210/pdb6jqv/pdb
• 分子名称: NAP1-related protein 2 (1 entity in total)
• 機能のキーワード: nucleosome assembly protein nrp2 nap nrp, chaperone
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49416.78

構造登録者

Kumar, A.,Vasudevan, D. (登録日: 2019-04-01, 公開日: 2019-07-10, 最終更新日: 2023-11-22)

主引用文献

Kumar, A.,Kumar Singh, A.,Chandrakant Bobde, R.,Vasudevan, D.
Structural Characterization ofArabidopsis thalianaNAP1-Related Protein 2 (AtNRP2) and Comparison with its Homolog AtNRP1.
Molecules, 24:-, 2019

PubMed Abstract: Nucleosome Assembly Protein (NAP) is a highly conserved family of histone chaperones present in yeast, animals, and plants. Unlike other organisms, plants possess an additional class of proteins in its NAP family, known as the NAP1-related proteins or NRP. possesses two NRP isoforms, namely AtNRP1 and AtNRP2, that share 87% sequence identity. Both AtNRP1 and AtNRP2 get expressed in all the plant tissues. Most works in the past, including structural studies, have focused on AtNRP1. We wanted to do a comparative study of the two proteins to find why the plant would have two very similar proteins and whether there is any difference between the two for their structure and function as histone chaperones. Here we report the crystal structure of AtNRP2 and a comparative analysis of its structural architecture with other NAP family proteins. The crystal structure of AtNRP2 shows it to be a homodimer, with its fold similar to that of other structurally characterized NAP family proteins. Although AtNRP1 and AtNRP2 have a similar fold, upon structural superposition, we find an offset in the dimerization helix of the two proteins. We evaluated the stability, oligomerization status, and histone chaperoning properties of the two proteins, for a comparison. The thermal melting experiments suggest that AtNRP2 is more stable than AtNRP1 at higher temperatures. In addition, electrophoretic mobility shift assay and isothermal titration calorimetry experiments suggest histone binding ability of AtNRP2 is higher than that of AtNRP1. Overall, these results provide insights about the specific function and relevance of AtNRP2 in plants through structural and biophysical studies.

PubMed: 31213016
DOI: 10.3390/molecules24122258

実験手法

X-RAY DIFFRACTION (3.42 Å)