Structural similarity in the DNA-binding domains of catabolite gene activator and cro repressor proteins.
Structural similarity in the DNA-binding domains of catabolite gene activator and cro repressor proteins.
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分解代谢物基因激活剂和 cro 阻遏蛋白的 DNA 结合域的结构相似性。
DOI：
10.1073/pnas.79.10.3097
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发表时间：
1982
影响因子：
11.1
通讯作者：
Matthews,BW
中科院分区：
文献类型：
--
作者：
Steitz,TA;Ohlendorf,DH;McKay,DB;Anderson,WF;Matthews,BW
结果表明，大肠杆菌分解代谢基因激活蛋白(CAP)的DNA结合区与噬菌体Lambda的CRO抑制蛋白(CRO)在结构上存在相似性。对于由两个连续的α-螺旋组成的结构单位来说，这两种蛋白质之间的对应关系尤其令人震惊。组成两个蛋白质中两个螺旋结构单元的24个α-碳原子可以叠加，均方根不一致为1.1A。这表明这一一致不太可能是由于偶然的对应。对于CAP激活蛋白和CRO抑制蛋白，它是两个螺旋单位的第二个α-螺旋，分别被认为结合在左手或右手B DNA的主要凹槽内[McKay，D.B.&Steitz，T.A.(1981)Nature(London)290,744-749；Anderson，W.F.，Ohlendorf，D.H.，Takeda，Y.&Matthews，B.W.(1981)Nature(London)290,754-758]。这里看到的CAP和CRO之间的结构对应，以及最近其他证据表明CRO、CAP和其他结合双链DNA的蛋白质之间的序列同源性，表明双螺旋单位可能是许多DNA结合蛋白的共同特征。结果还表明，特定蛋白质-双链DNA相互作用的一些原理可能是通用的，包括通过与DNA主沟相匹配的α-螺旋进行识别。
It is shown that there is a structural similarity between the presumed DNA-binding regions of the Escherichia coli catabolite gene activator protein ("CAP") and the cro repressor protein ("cro") from bacteriophage lambda. The correspondence between the two proteins is particularly striking for a structural unit consisting of two consecutive alpha-helices. The 24 alpha-carbon atoms that constitute the two-helical structural units in the two proteins can be superimposed with a root-mean-square disagreement of 1.1 A. It is shown that this agreement is very unlikely to be due to a chance correspondence. For both CAP activator and cro repressor proteins it is the second alpha-helix of the two-helical unit that has been proposed to bind within the major groove of left-handed or right-handed B DNA, respectively [McKay, D. B. & Steitz, T. A. (1981) Nature (London) 290, 744-749; Anderson, W. F., Ohlendorf, D. H., Takeda, Y. & Matthews, B. W. (1981) Nature (London) 290, 754-758]. The structural correspondence between CAP and cro seen here, together with other recent evidence of sequence homologies between cro, CAP, and other proteins that bind double-stranded DNA, suggests that the two-helical unit is likely to be a common feature of many DNA-binding proteins. The results also suggest that some principles of specific protein-double-stranded DNA interaction may be general and include recognition via alpha-helices fitting into the major groove of the DNA.