PDBsum entry 2k07

Structural genomics, unknown function

PDB id: 2k07

Contents

Protein chain

175 a.a. *

* Residue conservation analysis

PDB id:

2k07

Name:

Structural genomics, unknown function

Title:

Solution nmr structure of human e2-like ubiquitin-fold modifier conjugating enzyme 1 (ufc1). Northeast structural genomics consortium target hr41

Structure:

Ufm1-conjugating enzyme 1. Chain: a. Synonym: ubiquitin-fold modifier-conjugating enzyme 1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ufc1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

G.Liu,A.Eletsky,H.S.Atreya,J.M.Aramini,R.Xiao,T.Acton,G.T.Montelione, T.Szyperski,Northeast Structural Genomics Consortium (Nesg)

Key ref:

G.Liu et al. (2009). 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 Genomics, 10, 127-136. PubMed id: 19101823

Date:

25-Jan-08 Release date: 19-Feb-08

Supersedes:

1ywz

Protein chain

Q9Y3C8  (UFC1_HUMAN) -  Ubiquitin-fold modifier-conjugating enzyme 1 from Homo sapiens

Seq: 167 a.a.

Struc: 175 a.a.

Enzyme reactions

• Enzyme class: E.C.?

J Struct Funct Genomics 10:127-136 (2009)

PubMed id: 19101823

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.

G.Liu, F.Forouhar, A.Eletsky, H.S.Atreya, J.M.Aramini, R.Xiao, Y.J.Huang, M.Abashidze, J.Seetharaman, J.Liu, B.Rost, T.Acton, G.T.Montelione, J.F.Hunt, T.Szyperski.

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.