5gqt

Crystal structure of a specifier Protein from Arabidopsis thaliana

spinqualitylabelsall models 5gqt, resolution 3.02Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5gqt is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.022Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function JAL28_ARATH Responsible for constitutive and herbivore-induced simple nitrile formation. Promotes simple nitriles, but not epithionitrile or thiocyanate formation. Converts allylglucosinolate, 4-methylsulfinylbutylglucosinolate, 4-methylthiobutylglucosinolate and benzylglucosinolate to their corresponding simple nitriles in the presence of myrosinase. Publication Abstract from PubMed As important components of the glucosinolate-myrosinase system, specifier proteins mediate plant defense against herbivory and pathogen attacks. After tissue disruption, glucosinolates are hydrolyzed by myrosinases to instable aglucones, which will rearrange to form defensive isothiocyanates. Nevertheless, this reaction could be redirected to form other products by specifier proteins. Up to now, identified specifier proteins include epithiospecifier proteins (ESPs), thiocyanate forming proteins (TFPs), and nitrile-specifier proteins (NSPs). Recently, the structures of ESP and TFP have been reported. However, both the structure and the catalytic mechanism of NSPs remain enigmatic. Here, we solved the crystal structure of the NSP1 protein from Arabidopsis thaliana (AtNSP1). Structural comparisons with ESP and TFP proteins revealed several structural features of AtNSP1 different from those of the two proteins. Subsequent molecular docking studies showed that the R292 residue in AtNSP1 displayed a conformation different from those of the corresponding residues in ESP and TFP proteins, which might account for the product specificity and catalytic mechanism of AtNSP1. Taken together, the present study provides important insights into the molecular mechanisms underlying the different product spectrums between NSPs and the other two types of specifier proteins, and shed light on the future studies of the detailed mechanisms of other specifier proteins. Crystal structure of the nitrile-specifier protein NSP1 from Arabidopsis thaliana.,Zhang W, Zhou Y, Wang K, Dong Y, Wang W, Feng Y Biochem Biophys Res Commun. 2017 Jun 17;488(1):147-152. doi:, 10.1016/j.bbrc.2017.05.027. Epub 2017 May 4. PMID:28479247 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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