6RIZ
Crystal structure of gp41-1 intein (C1A, F65W, D107C)
6RIZ の概要
| エントリーDOI | 10.2210/pdb6riz/pdb |
| 分子名称 | gp41-1 intein (2 entities in total) |
| 機能のキーワード | intein, protein-splicing, splicing, hydrolase |
| 由来する生物種 | metagenome |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 14437.58 |
| 構造登録者 | Beyer, H.M.,Lountos, G.T.,Mikula, M.K.,Wlodawer, A.,Iwai, H. (登録日: 2019-04-25, 公開日: 2020-04-29, 最終更新日: 2024-10-23) |
| 主引用文献 | Beyer, H.M.,Virtanen, S.I.,Aranko, A.S.,Mikula, K.M.,Lountos, G.T.,Wlodawer, A.,Ollila, O.H.S.,Iwai, H. The Convergence of the Hedgehog/Intein Fold in Different Protein Splicing Mechanisms. Int J Mol Sci, 21:-, 2020 Cited by PubMed Abstract: Protein splicing catalyzed by inteins utilizes many different combinations of amino-acid types at active sites. Inteins have been classified into three classes based on their characteristic sequences. We investigated the structural basis of the protein splicing mechanism of class 3 inteins by determining crystal structures of variants of a class 3 intein from and molecular dynamics simulations, which suggested that the class 3 intein utilizes a different splicing mechanism from that of class 1 and 2 inteins. The class 3 intein uses a bond cleavage strategy reminiscent of proteases but share the same Hedgehog/INTein (HINT) fold of other intein classes. Engineering of class 3 inteins from a class 1 intein indicated that a class 3 intein would unlikely evolve directly from a class 1 or 2 intein. The HINT fold appears as structural and functional solution for -peptidyl and -esterification reactions commonly exploited by diverse mechanisms using different combinations of amino-acid types for the active-site residues. PubMed: 33171880DOI: 10.3390/ijms21218367 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.85 Å) |
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