Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM structure and rational engineering of a superefficient ochratoxin A-detoxifying amidohydrolase.
Journal, issue, pages	J Hazard Mater, Vol. 458, Page 131836, Year 2023
Publish date	Sep 15, 2023
Authors	Longhai Dai / Du Niu / Jian-Wen Huang / Xian Li / Panpan Shen / Hao Li / Zhenzhen Xie / Jian Min / Yumei Hu / Yu Yang / Rey-Ting Guo / Chun-Chi Chen /
PubMed Abstract	Ochratoxin A (OTA) is among the most prevalent mycotoxins detected in agroproducts, posing serious threats to human and livestock health. Using enzymes to conduct OTA detoxification is an appealing ...Ochratoxin A (OTA) is among the most prevalent mycotoxins detected in agroproducts, posing serious threats to human and livestock health. Using enzymes to conduct OTA detoxification is an appealing potential strategy. The recently identified amidohydrolase from Stenotrophomonas acidaminiphila, termed ADH3, is the most efficient OTA-detoxifying enzyme reported thus far and can hydrolyze OTA to nontoxic ochratoxin α (OTα) and L-β-phenylalanine (Phe). To elucidate the catalytic mechanism of ADH3, we solved the single-particle cryo-electron microscopy (cryo-EM) structures of apo-form, Phe- and OTA-bound ADH3 to an overall resolution of 2.5-2.7 Å. The role of OTA-binding residues was investigated by structural, mutagenesis and biochemical analyses. We also rationally engineered ADH3 and obtained variant S88E, whose catalytic activity was elevated by 3.7-fold. Structural analysis of variant S88E indicates that the E88 side chain provides additional hydrogen bond interactions to the OTα moiety. Furthermore, the OTA-hydrolytic activity of variant S88E expressed in Pichia pastoris is comparable to that of Escherichia coli-expressed enzyme, revealing the feasibility of employing the industrial yeast strain to produce ADH3 and its variants for further applications. These results unveil a wealth of information about the catalytic mechanism of ADH3-mediated OTA degradation and provide a blueprint for rational engineering of high-efficiency OTA-detoxifying machineries.
External links	J Hazard Mater / PubMed:37331057
Methods	EM (single particle)
Resolution	2.5 - 2.71 Å
Structure data	35452 8ihq EMDB-35452, PDB-8ihq: Cryo-EM structure of ochratoxin A-detoxifying amidohydrolase ADH3 Method: EM (single particle) / Resolution: 2.71 Å 35453 8ihr EMDB-35453, PDB-8ihr: Cryo-EM structure of ochratoxin A-detoxifying amidohydrolase ADH3 in complex with Phe Method: EM (single particle) / Resolution: 2.5 Å 35454 8ihs EMDB-35454, PDB-8ihs: Cryo-EM structure of ochratoxin A-detoxifying amidohydrolase ADH3 in complex with ochratoxin A Method: EM (single particle) / Resolution: 2.5 Å 36060 8j85 EMDB-36060, PDB-8j85: Cryo-EM structure of ochratoxin A-detoxifying amidohydrolase ADH3 mutant S88E in complex with ochratoxin A Method: EM (single particle) / Resolution: 2.7 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-PHE: PHENYLALANINE ChemComp-97U: (2~{S})-2-[[(3~{R})-5-chloranyl-3-methyl-8-oxidanyl-1-oxidanylidene-3,4-dihydroisochromen-7-yl]carbonylamino]-3-phenyl-propanoic acid / toxin*YM
Source	stenotrophomonas acidaminiphila (bacteria)
Keywords	HYDROLASE / amidohydrolase / octamer / ochratoxin A degradtion / cryo-EM structure