Crystallographic snapshots of the EF-hand protein MCFD2 complexed with the intracellular lectin ERGIC-53 involved in glycoprotein transport.,Acta Crystallographica Section F

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Crystallographic snapshots of the EF-hand protein MCFD2 complexed with the intracellular lectin ERGIC-53 involved in glycoprotein transport.
Acta Crystallographica Section F ( IF 1.1 ) Pub Date : 2020-05-01 , DOI: 10.1107/s2053230x20005452
Tadashi Satoh ₁ , Miho Nishio ₁ , Kousuke Suzuki ₁ , Maho Yagi-Utsumi ₁ , Yukiko Kamiya ₁ , Tsunehiro Mizushima ₁ , Koichi Kato ₁

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The transmembrane intracellular lectin ER–Golgi intermediate compartment protein 53 (ERGIC‐53) and the soluble EF‐hand multiple coagulation factor deficiency protein 2 (MCFD2) form a complex that functions as a cargo receptor, trafficking various glycoproteins between the endoplasmic reticulum (ER) and the Golgi apparatus. It has been demonstrated that the carbohydrate‐recognition domain (CRD) of ERGIC‐53 (ERGIC‐53^CRD) interacts with N‐linked glycans on cargo glycoproteins, whereas MCFD2 recognizes polypeptide segments of cargo glycoproteins. Crystal structures of ERGIC‐53^CRD complexed with MCFD2 and mannosyl oligosaccharides have revealed protein–protein and protein–sugar binding modes. In contrast, the polypeptide‐recognition mechanism of MCFD2 remains largely unknown. Here, a 1.60 Å resolution crystal structure of the ERGIC‐53^CRD–MCFD2 complex is reported, along with three other crystal forms. Comparison of these structures with those previously reported reveal that MCFD2, but not ERGIC‐53–CRD, exhibits significant conformational plasticity that may be relevant to its accommodation of various polypeptide ligands.

中文翻译：

EF 手蛋白 MCFD2 与参与糖蛋白转运的细胞内凝集素 ERGIC-53 复合的晶体快照。

跨膜细胞内凝集素 ER-高尔基中间室蛋白 53 (ERGIC-53) 和可溶性 EF-hand 多重凝血因子缺陷蛋白 2 (MCFD2) 形成复合物，充当货物受体，在内质网 (ER) 之间运输各种糖蛋白）和高尔基体。已经证明，ERGIC-53 的碳水化合物识别结构域 (CRD) (ERGIC-53 ^CRD ) 与货物糖蛋白上的 N 连接聚糖相互作用，而 MCFD2 识别货物糖蛋白的多肽片段。^{ERGIC-53 CRD}与 MCFD2 和甘露糖寡糖复合的晶体结构揭示了蛋白质-蛋白质和蛋白质-糖结合模式。相比之下，MCFD2 的多肽识别机制仍然很大程度上未知。在此，报道了 ERGIC-53 ^CRD -MCFD2 复合物的 1.60 Å 分辨率晶体结构，以及其他三种晶体形式。这些结构与之前报道的结构的比较表明，MCFD2（而不是 ERGIC-53-CRD）表现出显着的构象可塑性，这可能与其对各种多肽配体的适应有关。

更新日期：2020-05-01

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