PDBsum entry 5gq0

Plant protein

PDB id: 5gq0

Contents

Protein chains

330 a.a.

Waters ×361

PDB id:

5gq0

Name:

Plant protein

Title:

Crystal structure of the epithiospecifier protein, esp from arabidopsis thaliana

Structure:

Epithiospecifier protein. Chain: b, a. Synonym: atesp,protein epithiospecifying senescence regulator,atesr. Engineered: yes

Source:

Arabidopsis thaliana. Mouse-ear cress. Organism_taxid: 3702. Gene: esp, esr, tasty, at1g54040, f15i1.12. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.31Å R-factor: 0.191 R-free: 0.231

Authors:

W.Zhang,Y.Feng

Key ref:

W.Zhang et al. (2016). Crystal structure of the Epithiospecifier Protein, ESP from Arabidopsis thaliana provides insights into its product specificity. Biochem Biophys Res Commun, 478, 746-751. PubMed id: 27498030 DOI: 10.1016/j.bbrc.2016.08.019

Date:

05-Aug-16 Release date: 17-Aug-16

Protein chains

Q8RY71  (ESP_ARATH) -  N-(sulfonatooxy)alkenimidothioic acid sulfate-lyase (epithionitrile-forming) from Arabidopsis thaliana

Seq: 341 a.a.

Struc: 330 a.a.

Enzyme reactions

• Enzyme class 1: E.C.4.8.1.5 - thiohydroximate-O-sulfate sulfate/sulfur-lyase (nitrile-forming).
• Reaction: a (Z)-N-(sulfonatooxy)alkanimidothioate = a nitrile + sulfur + sulfate
• Enzyme class 2: E.C.4.8.1.6 - N-(sulfonatooxy)alkenimidothioic acid sulfate-lyase (epithionitrile-
• Reaction: a (Z)-N-(sulfonatooxy)alkenimidothioate = an epithionitrile + sulfate

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.bbrc.2016.08.019

Biochem Biophys Res Commun 478:746-751 (2016)

PubMed id: 27498030

Crystal structure of the Epithiospecifier Protein, ESP from Arabidopsis thaliana provides insights into its product specificity.

W.Zhang, W.Wang, Z.Liu, Y.Xie, H.Wang, Y.Mu, Y.Huang, Y.Feng.

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.