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Identification of residues for chaperone-like activity of OppA protein in Yersinia pseudotuberculosis.
AMB Express ( IF 3.7 ) Pub Date : 2020-08-21 , DOI: 10.1186/s13568-020-01090-8
Elena Escobar Garduño 1 , Thomas Scior 2 , Lucia Soto Urzúa 1 , Luis Javier Martínez Morales 1
Affiliation  

Periplasmic oligopeptide binding protein (OppA) is part of a multimeric cytoplasmic membrane protein complex, whose function is known as peptide transporters found in Gram-negative bacteria. A chaperone-like activity has been found for the OppA from Yersinia pseudotuberculosis, using biochemical experiments. Through computational analysis, we selected two amino acid residues (R41 and D42) that probably are involved in the chaperone-like activity. Our results to corroborate how OppA assists refolding and renaturation of lactate dehydrogenase and alpha-glucosidase denatured enzymes.

中文翻译:

鉴定耶尔森氏菌假结核耶尔森菌中OppA蛋白伴侣样活性的残基。

周质寡肽结合蛋白(OppA)是多聚体胞质膜蛋白复合物的一部分,其功能被称为革兰氏阴性细菌中的肽转运蛋白。使用生化实验,已经发现假性耶尔森氏菌的OppA具有类似伴侣的活性。通过计算分析,我们选择了可能与伴侣蛋白样活性有关的两个氨基酸残基(R41和D42)。我们的结果证实了OppA如何帮助乳酸脱氢酶和α-葡萄糖苷酶变性酶重新折叠和复性。
更新日期:2020-08-21
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