کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1930485 1050516 2011 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Role of aromatic stack pairing at the catalytic site of gelonin protein
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Role of aromatic stack pairing at the catalytic site of gelonin protein
چکیده انگلیسی

Aromatic–aromatic interactions play an important role in the enzyme–substrate recognition mechanism and in stabilization of proteins. Gelonin – a ribosome inactivating protein (RIP) from the plant Gelonium multiflorum – belongs to type-I RIPs and shows N-glycosylation activity which has been used as a model to explain the role of aromatic–aromatic stack pairing in RIPs. RIPs have a different substrate binding site and catalytic site. Role of tyrosine residues at the binding site has already been known but the role of tyrosine residues at catalytic site is still unclear. In this study, the role of tyrosine–adenine–tyrosine aromatic stack pairing at the catalytic site was studied by in silico mutation studies using molecular dynamic simulations. Through this study we report that, despite the fact that aromatic stack pairing aids in recognition of adenine at binding site, both the tyrosine residues of stack pairing play a crucial role in the stabilization of adenine at catalytic site. In the absence of both the tyrosine residues, adenine was unstable at catalytic site that results in the inhibition of N-glycosylation activity of gelonin protein. Hence, this study highlights the importance of π–π stack pairing in the N-glycosidic activity of gelonin by determining its role in stabilizing adenine at catalytic site.


► This study highlights the importance of π–π interactions at the catalytic site of ribosome inactivating proteins (RIP).
► In silico mutation studies using molecular dynamics simulation revealed that π–π stack pairing plays a key role in N-glycosylation activity of RIP.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 410, Issue 1, 24 June 2011, Pages 75–80
نویسندگان
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