2K07

Solution NMR structure of human E2-like ubiquitin-fold modifier conjugating enzyme 1 (UFC1). Northeast Structural Genomics Consortium target HR41

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2K07 の概要

• エントリーDOI: 10.2210/pdb2k07/pdb
• 分子名称: Ufm1-conjugating enzyme 1 (1 entity in total)
• 機能のキーワード: ufc1, ubiquitin conjugating enzyme, e2, ufm1, polymorphism, ubl conjugation pathway, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, unknown function
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20557.55

構造登録者

Liu, G.,Eletsky, A.,Atreya, H.S.,Aramini, J.M.,Xiao, R.,Acton, T.,Montelione, G.T.,Szyperski, T.,Northeast Structural Genomics Consortium (NESG) (登録日: 2008-01-25, 公開日: 2008-02-19, 最終更新日: 2024-05-29)

主引用文献

Liu, G.,Forouhar, F.,Eletsky, A.,Atreya, H.S.,Aramini, J.M.,Xiao, R.,Huang, Y.J.,Abashidze, M.,Seetharaman, J.,Liu, J.,Rost, B.,Acton, T.,Montelione, G.T.,Hunt, J.F.,Szyperski, T.
NMR and X-RAY structures of human E2-like ubiquitin-fold modifier conjugating enzyme 1 (UFC1) reveal structural and functional conservation in the metazoan UFM1-UBA5-UFC1 ubiquination pathway.
J.STRUCT.FUNCT.GENOM., 10:127-136, 2009

PubMed Abstract: For cell regulation, E2-like ubiquitin-fold modifier conjugating enzyme 1 (Ufc1) is involved in the transfer of ubiquitin-fold modifier 1 (Ufm1), a ubiquitin like protein which is activated by E1-like enzyme Uba5, to various target proteins. Thereby, Ufc1 participates in the very recently discovered Ufm1-Uba5-Ufc1 ubiquination pathway which is found in metazoan organisms. The structure of human Ufc1 was solved by using both NMR spectroscopy and X-ray crystallography. The complementary insights obtained with the two techniques provided a unique basis for understanding the function of Ufc1 at atomic resolution. The Ufc1 structure consists of the catalytic core domain conserved in all E2-like enzymes and an additional N-terminal helix. The active site Cys(116), which forms a thio-ester bond with Ufm1, is located in a flexible loop that is highly solvent accessible. Based on the Ufc1 and Ufm1 NMR structures, a model could be derived for the Ufc1-Ufm1 complex in which the C-terminal Gly(83) of Ufm1 may well form the expected thio-ester with Cys(116), suggesting that Ufm1-Ufc1 functions as described for other E1-E2-E3 machineries. alpha-helix 1 of Ufc1 adopts different conformations in the crystal and in solution, suggesting that this helix plays a key role to mediate specificity.

PubMed: 19101823
DOI: 10.1007/s10969-008-9054-7

実験手法

SOLUTION NMR