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Complex structure of the acyltransferase VinK and the carrier protein VinL with a pantetheine cross-linking probe
Acta Crystallographica Section F ( IF 1.072 ) Pub Date : 2021-09-02 , DOI: 10.1107/s2053230x21008761
Akimasa Miyanaga 1 , Risako Ouchi 1 , Fumitaka Kudo 1 , Tadashi Eguchi 1
Affiliation  

Acyltransferases are responsible for the selection and loading of acyl units onto carrier proteins in polyketide and fatty-acid biosynthesis. Despite the importance of protein–protein interactions between the acyltransferase and the carrier protein, structural information on acyltransferase–carrier protein interactions is limited because of the transient interactions between them. In the biosynthesis of the polyketide vicenistatin, the acyltransferase VinK recognizes the carrier protein VinL for the transfer of a dipeptidyl unit. The crystal structure of a VinK–VinL covalent complex formed with a 1,2-bismaleimidoethane cross-linking reagent has been determined previously. Here, the crystal structure of a VinK–VinL covalent complex formed with a pantetheine cross-linking probe is reported at 1.95 Å resolution. In the structure of the VinK–VinL–probe complex, the pantetheine probe that is attached to VinL is covalently connected to the side chain of the mutated Cys106 of VinK. The interaction interface between VinK and VinL is essentially the same in the two VinK–VinL complex structures, although the position of the pantetheine linker slightly differs. This structural observation suggests that interface interactions are not affected by the cross-linking strategy used.

中文翻译:

酰基转移酶 VinK 和载体蛋白 VinL 的复杂结构与泛硫胺交联探针

酰基转移酶负责在聚酮化合物和脂肪酸生物合成中选择和装载酰基单元到载体蛋白上。尽管酰基转移酶和载体蛋白之间的蛋白质-蛋白质相互作用很重要,但由于它们之间的瞬时相互作用,有关酰基转移酶-载体蛋白相互作用的结构信息是有限的。在聚酮化合物维司他丁的生物合成中,酰基转移酶 VinK 识别载体蛋白 VinL 以转移二肽基单元。先前已经确定了与 1,2-双马来酰亚胺乙烷交联剂形成的 VinK-VinL 共价复合物的晶体结构。在这里,以 1.95 Å 的分辨率报告了与泛替硫因交联探针形成的 VinK-VinL 共价复合物的晶体结构。在VinK-VinL-探针复合物的结构中,附着在VinL上的泛泰硫因探针与VinK突变的Cys106侧链共价连接。VinK 和 VinL 之间的相互作用界面在两个 VinK-VinL 复合结构中基本相同,尽管泛太碱连接子的位置略有不同。这种结构观察表明界面相互作用不受所使用的交联策略的影响。
更新日期:2021-09-02
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