Abstract：
Methylcrotonyl-CoA carboxylase (MCCC) is a biotin dependent enzyme, that plays a crucial role in leucine metabolism. The enzyme comprises a biotin carboxylase (BC), a carboxyltransferase (CT), and a biotin carboxyl carrier protein (BCCP) domain. MCCC is synthesized as an apo-protein, and is posttranslationally modified at a lysine residue, conserved in the biotin carboxyl carrier protein (BCCP) domain. In order to understand the structure, function and interactions of L. major MCCC, we have expressed and characterized its domains. Here we report the complete chemical shift assignments of MCCC BCCP domain of L. major. Furthermore, we have used the assignments to generate a model of the same, using CS-Rosetta. We have also followed its chemical shift perturbations upon biotin modification. Changes were observed at the lysine 51 amide, that undergoes biotin modification, and a few others present in its immediate neighborhood.
摘要：
甲基巴豆酰辅酶A羧化酶（MCCC）是一种生物素依赖性酶，在亮氨酸代谢中起着至关重要的作用。该酶包括生物素羧化酶（BC），羧化酶（CT），和生物素羧基载体蛋白(BCCP)结构域。MCCC是作为apo蛋白合成的，并在赖氨酸残基处进行翻译后修饰，在生物素羧基载体蛋白（BCCP）结构域中保守。为了理解结构，L.majorMCCC的功能和相互作用，我们已经表达和表征了它的领域。在这里，我们报告了L.major的MCCCBCCP域的完整化学位移分配。此外，我们已经使用赋值来生成相同的模型，使用CS-Rosetta。我们还跟踪了生物素修饰后的化学位移扰动。在赖氨酸51酰胺处观察到变化，经过生物素修饰，和其他几个人在它的附近。
