5GQ0

Crystal structure of the Epithiospecifier Protein, ESP from Arabidopsis thaliana

Summary for 5GQ0

• Entry DOI: 10.2210/pdb5gq0/pdb
• Descriptor: Epithiospecifier protein (2 entities in total)
• Functional Keywords: specifier protein, beta sheet, beta propeller, plant protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Cellular location: Cytoplasm : Q8RY71
• Total number of polymer chains: 2
• Total formula weight: 76236.55

Authors

Zhang, W.,Feng, Y. (deposition date: 2016-08-05, release date: 2016-08-17, Last modification date: 2023-11-08)

Primary citation

Zhang, W.,Wang, W.,Liu, Z.,Xie, Y.,Wang, H.,Mu, Y.,Huang, Y.,Feng, Y.
Crystal structure of the Epithiospecifier Protein, ESP from Arabidopsis thaliana provides insights into its product specificity
Biochem.Biophys.Res.Commun., 478:746-751, 2016

PubMed Abstract: Specifier proteins are important components of the glucosinolate-myrosinase system, which mediate plant defense against herbivory and pathogen attacks. Upon tissue disruption, glucosinolates are hydrolyzed to instable aglucones by myrosinases, and then aglucones will rearrange to form defensive isothiocyanates. Specifier proteins can redirect this reaction to form other products, such as simple nitriles, epithionitriles and organic thiocyanates instead of isothiocyanates based on the side chain structure of glucosinolate and the type of the specifier proteins. Nevertheless, the molecular mechanism underlying the different product spectrums of various specifier proteins was not fully understood. Here in this study, we solved the crystal structure of the Epithiospecifier Protein, ESP from Arabidopsis thaliana (AtESP) at 2.3 Å resolution. Structural comparisons with the previously solved structure of thiocyanate forming protein, TFP from Thlaspi arvense (TaTFP) reveal that AtESP shows a dimerization pattern different from TaTFP. Moreover, AtESP harbors a slightly larger active site pocket than TaTFP and several residues around the active site are different between the two proteins, which might account for the different product spectrums of the two proteins. Together, our structural study provides important insights into the molecular mechanisms of specifier proteins and shed light on the basis of their different product spectrums.

PubMed: 27498030
DOI: 10.1016/j.bbrc.2016.08.019

Experimental method

X-RAY DIFFRACTION (2.31 Å)