Unknown

Dataset Information

0

Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7).

ABSTRACT: The human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7) is involved in protein degradation, including a process known as endoplasmic reticulum-associated degradation (ERAD). The crystal structure of human UBE2G2/UBC7 was solved at 2.56 angstroms resolution. The UBE2G2 structure comprises a single domain consisting of an antiparallel beta-sheet with four strands, five alpha-helices and two 3(10)-helices. Structural comparison of human UBE2G2 with yeast Ubc7 indicated that the overall structures are similar except for the long loop region and the C-terminal helix. Superimposition of UBE2G2 on UbcH7 in a c-Cbl-UbcH7-ZAP70 ternary complex suggested that the two loop regions of UBE2G2 interact with the RING domain in a similar way to UbcH7. In addition, the extra loop region of UBE2G2 may interact with the RING domain or its neighbouring region and may be involved in the binding specificity and stability.

SUBMITTER: Arai R 

PROVIDER: S-EPMC2222581 | biostudies-literature | 2006 Apr

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7).

Arai Ryoichi R   Yoshikawa Seiko S   Murayama Kazutaka K   Imai Yuzuru Y   Takahashi Ryosuke R   Shirouzu Mikako M   Yokoyama Shigeyuki S  

Acta crystallographica. Section F, Structural biology and crystallization communications 20060325 Pt 4

The human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7) is involved in protein degradation, including a process known as endoplasmic reticulum-associated degradation (ERAD). The crystal structure of human UBE2G2/UBC7 was solved at 2.56 angstroms resolution. The UBE2G2 structure comprises a single domain consisting of an antiparallel beta-sheet with four strands, five alpha-helices and two 3(10)-helices. Structural comparison of human UBE2G2 with yeast Ubc7 indicated that the overall structure  ...[more]

Similar Datasets

Unknown Solution structure and dynamics of human ubiquitin conjugating enzyme Ube2g2.
| S-EPMC2822102 | biostudies-literature
Unknown Mechanism of polyubiquitin chain recognition by the human ubiquitin conjugating enzyme Ube2g2.
| S-EPMC3030398 | biostudies-literature
Unknown A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-function screen.
| S-EPMC3412965 | biostudies-literature
Unknown Conformational Dynamics Modulate Activation of the Ubiquitin Conjugating Enzyme Ube2g2.
| S-EPMC5579538 | biostudies-literature
Unknown Analysis of the human E2 ubiquitin conjugating enzyme protein interaction network.
| S-EPMC2765280 | biostudies-literature
Unknown Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2.
| S-EPMC2644258 | biostudies-literature
Unknown Structure of full-length ubiquitin-conjugating enzyme E2-25K (huntingtin-interacting protein 2).
| S-EPMC2675580 | biostudies-literature
Unknown RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination.
| S-EPMC18039 | biostudies-literature
Unknown Design, synthesis, and anticancer activity evaluation of irreversible allosteric inhibitors of the ubiquitin-conjugating enzyme Ube2g2.
| S-EPMC6238722 | biostudies-literature
Unknown Ancient ubiquitous protein 1 (AUP1) localizes to lipid droplets and binds the E2 ubiquitin conjugase G2 (Ube2g2) via its G2 binding region.
| S-EPMC3037673 | biostudies-literature