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-Structure paper
タイトル | A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin. |
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ジャーナル・号・ページ | Int J Biol Macromol, Vol. 118, Issue Pt A, Page 671-675, Year 2018 |
掲載日 | 2018年10月15日 |
著者 | Ramanathan Natesh / Daniel K Clare / George W Farr / Arthur L Horwich / Helen R Saibil / |
PubMed 要旨 | 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 ...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. |
リンク | Int J Biol Macromol / PubMed:29959019 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 11.0 - 12.2 Å |
構造データ | EMDB-6725: EMDB-6726: EMDB-6727: |
由来 |
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