3EVX

Crystal structure of the human E2-like ubiquitin-fold modifier conjugating enzyme 1 (Ufc1). Northeast Structural Genomics Consortium target HR41

Replaces:  2IN1Replaces:  3E2G

Summary for 3EVX

• Entry DOI: 10.2210/pdb3evx/pdb
• Descriptor: Ufm1-conjugating enzyme 1, THIOCYANATE ION (3 entities in total)
• Functional Keywords: alpha-beta protein, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, polymorphism, ubl conjugation pathway, ligase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 4
• Total formula weight: 83025.26

Authors

Forouhar, F.,Abashidze, M.,Seetharaman, J.,Ho, C.K.,Janjua, H.,Cunningham, K.,Ma, L.-C.,Xiao, R.,Baran, M.C.,Acton, T.B.,Rost, B.,Montelione, G.T.,Tong, L.,Hunt, J.F.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2008-10-13, release date: 2008-10-21, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.54 Å)