Format

Send to

Choose Destination
Spectrochim Acta A Mol Biomol Spectrosc. 2017 Feb 15;173:1001-1006. doi: 10.1016/j.saa.2016.10.044. Epub 2016 Oct 24.

Spectroscopic and molecular docking study on the interaction between salicylic acid and the induced disease-resistant protein OsAAA1 of rice.

Author information

1
Hubei Provincial Key Laboratory for Protection and Application of Special Plants in Wuling Area of China, College of Life Science, South-Central University for Nationalities, Wuhan 430074, China.
2
College of Pharmacy, South-Central University for Nationalities, Wuhan 430074, China.
3
Academy of Agricultural Sciences of Jingzhou, Jingzhou 434000, China.
4
Hubei Provincial Key Laboratory for Protection and Application of Special Plants in Wuling Area of China, College of Life Science, South-Central University for Nationalities, Wuhan 430074, China. Electronic address: liuxinqiong@mail.scuec.edu.cn.

Abstract

The interaction between salicylic acid (SA) and the induced disease-resistant protein OsAAA1 in rice was studied using spectroscopy and molecular docking. Ultraviolet (UV) absorption spectroscopy demonstrated an interaction between OsAAA1 protein and SA. Spectroscopy showed that this interaction was a dynamic quenching process. Synchronous fluorescence spectroscopy (SFS) further revealed that this interaction caused changes in the microenvironment of tyrosine and tryptophan and that the interaction site was closer to the tryptophan residue. The structural model of protein OsAAA1 was determined by homology modeling method, and the molecular docking simulation diagram of OsAAA1 with SA was obtained. These models, in combination with a Ramachandran plot analysis, showed amino acid residues ranging from position 240 to position 420 as the possible site interacting with SA. Among them, Gly389, Lys257 and Glu425 might be three key amino acids that can form hydrogen bonds with SA.

KEYWORDS:

Induced disease-resistant gene OsAAA1; Molecular docking; Salicylic acid; Spectroscopy

PMID:
28029507
DOI:
10.1016/j.saa.2016.10.044
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center