کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
8326881 1540196 2018 15 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin
چکیده انگلیسی
The chaperonins (GroEL and GroES in Escherichia coli) are ubiquitous molecular chaperones that assist a subset of essential substrate proteins to undergo productive folding to the native state. Using single particle cryo EM and image processing we have examined complexes of E. coli GroEL with the stringently GroE-dependent substrate enzyme RuBisCO from Rhodospirillum rubrum. Here we present snapshots of non-native RuBisCO - GroEL complexes. We observe two distinct substrate densities in the binary complex reminiscent of the two-domain structure of the RuBisCO subunit, so that this may represent a captured form of an early folding intermediate. The occupancy of the complex is consistent with the negative cooperativity of GroEL with respect to substrate binding, in accordance with earlier mass spectroscopy studies.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 118, Part A, 15 October 2018, Pages 671-675
نویسندگان
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