Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7)
Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7)
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DOI：
10.1107/s1744309106009006
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发表时间：
2006-04-01
影响因子：
0.9
通讯作者：
Yokoyama, S
中科院分区：
文献类型：
--
作者：
Arai, R;Yoshikawa, S;Yokoyama, S
人类泛素结合酶E2 G2(UBE2G2/UBC7)参与蛋白质降解，包括内质网相关降解(ERAD)。在2.56埃分辨率下对人UBE2G2/UBC7的晶体结构进行了解析。UBE2G2结构由一个由四条反平行的β-折叠、五个α-螺旋和两个3(10)-螺旋组成的单一结构域组成。人UBE2G2和酵母UBC7的结构比较表明，除了长环区和C末端螺旋外，其余结构相似。在c-Cbl-UbcH7-ZAP70三元络合物中，UBE2G2重叠在UbcH7上，表明UBE2G2的两个环区与环域的作用方式与UbcH7相似。此外，UBE2G2的额外环区可能与环区或其邻近区域相互作用，并可能参与结合的特异性和稳定性。
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 angstrom 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.