The function of the type II peptidyl carrier protein (PCP) ColA1a in collismycin (COL) biosynthesis was characterized in this study. ColA1a was involved in the selection and loading of picolinic acid (PA), instead of normal amino acid substrates, as the origin of ring B in COLs. The 2.1 Å crystal structure of ColA1a was solved. Primary and tertiary structural comparison of ColA1a with other PCPs revealed the structural basis for their typical α‐helical bundles. More details are discussed in the article by Ma et al. on page 963—969.

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内盖

在这项研究中表征了II型肽基载体蛋白（PCP）ColA1a在Collismycin（COL）生物合成中的功能。ColA1a参与了吡啶甲酸（PA）的选择和负载，而不是正常氨基酸的底物，是COL中B环的起源。解析了ColA1a的2.1Å晶体结构。ColA1a与其他PCP的一级和三级结构比较揭示了其典型α螺旋束的结构基础。Ma等人的文章中讨论了更多细节。在963—969页上。