CRYSTAL-STRUCTURE OF APO-NEOCARZINOSTATIN AT 0.15-NM RESOLUTION
CRYSTAL-STRUCTURE OF APO-NEOCARZINOSTATIN AT 0.15-NM RESOLUTION
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DOI：
10.1111/j.1432-1033.1993.tb17814.x
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发表时间：
1993-04-15
期刊：
影响因子：
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通讯作者：
KUROMIZU, K
中科院分区：
文献类型：
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作者：
TEPLYAKOV, A;OBMOLOVA, G;KUROMIZU, K
用0.15 nm分辨率的X射线衍射法测定了卡氏链霉菌抗肿瘤抗菌蛋白apo-neoczinostatin的三维结构，R=17.2%。新卡西诺斯汀的晶体结构与相关蛋白质放线黄质和大莫霉素相似。它与核磁共振波谱测定的溶液结构也是一致的。该蛋白质分子由一个七链反平行的β-三明治和一个由两个β-条带组成的较小的叶组成。两叶之间的深裂隙是一个假定的发色团结合部位。Trp39、Leu45、Phe5-、Phe78的侧链和排列新卡宾抑素结合裂隙的二硫键Cys37-Cys47表明疏水相互作用在稳定发色团分子中的重要性。通过比较新卡宾抑素、放线菌素和大莫霉素的原子模型，揭示了功能残基可能决定了对不同发色团的特异性。
The three-dimensional structure of apo-neocarzinostatin, an antitumour- antibiotic protein isolated from Streptomyces carzinostaticus, has been determined by X-ray diffraction at 0.15-nm resolution and refined to R = 17.2%. The crystal structure of neocarzinostin is similar to that of the related proteins actinoxanthin and macromomycin. It is also in good agreement with the solution structure determined by NMR spectroscopy. The protein molecule consists of a seven-stranded antiparallel beta-sandwich and a smaller lobe formed by two beta-ribbons. A deep cleft between the two lobes is a putative chromophore binding site. Side chains of Trp39, Leu45, Phe5-, Phe78 and the disulphide Cys37-Cys47 aligning the binding cleft in neocarzinostatin suggest the importance of hydrophobic interactions in stabilizing the chromophore molecule. Comparison of the atomic models of neocarzinostatin, actinoxanthin and macromomycin reveals functional residues which might determine specificity towards different chromophores.