Ubiquitination is a post-translational modification that regulates a plethora of processes in cells. Ubiquitination requires three type of enzyme: E1 ubiquitin (Ub) activating enzymes, E2 Ub conjugating enzymes and E3 ubiquitin ligases. The E2 enzymes perform a variety of functions, as Ub chain initiation, elongation and regulation of the topology and the process of chain formation. The E2 enzymes family is mainly characterized by a highly conserved ubiquitin conjugating domain (UBC), which comprises the binding region for the activated Ub, E1 and E3 enzymes. The E2 enzyme UbcH7 (UBE2L3) is a known interacting partner for different types of E3 Ub ligases such as HECT, RING and RBR. A structural analysis of the apo form of the native UbcH7 will provide the structural information to understand how this E2 enzyme is implicated in a wide range of diseases and how it interacts with its partners. In the present study we present the high yield expression of the native UbcH7 E2 enzyme and its preliminary analysis via solution NMR spectroscopy. The E2 enzyme is folded in solution and nearly a complete backbone assignment was achieved. Additionally, TALOS+ analysis was performed and the results indicated that UbcH7 adopts a αββββααα topology which is similar to that of the majority of E2 enzymes.

中文翻译：

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UbcH7（UBE2L3）天然形式的1H，13C，15N主链和侧链共振分配通过溶液NMR光谱法进行。

泛素化是翻译后修饰，其调节细胞中的过多过程。泛素化需要三种类型的酶：E1泛素（Ub）活化酶，E2 Ub缀合酶和E3泛素连接酶。E2酶具有多种功能，如Ub链引发，拓扑结构的延伸和调控以及链形成的过程。E2酶家族的主要特征是高度保守的泛素结合结构域（UBC），该结构域包含激活的Ub，E1和E3酶的结合区。E2酶UbcH7（UBE2L3）是不同类型的E3 Ub连接酶（例如HECT，RING和RBR）的已知相互作用伴侣。对天然UbcH7载脂蛋白形式的结构分析将提供结构信息，以了解这种E2酶如何与多种疾病有关以及如何与其伴侣相互作用。在本研究中，我们介绍了天然UbcH7 E2酶的高产量表达及其通过溶液NMR光谱进行的初步分析。E2酶在溶液中折叠，几乎实现了完整的骨架分配。此外，进行了TALOS +分析，结果表明UbcH7采用了αββββααα拓扑结构与大多数E2酶的拓扑结构相似。