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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >An additional C-terminal loop in endonuclease IV, an apurinic/apyrimidinic endonuclease, controls binding affinity to DNA.
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An additional C-terminal loop in endonuclease IV, an apurinic/apyrimidinic endonuclease, controls binding affinity to DNA.

机译：一个额外的c端循环在第四核酸内切酶,一个apurinic / apyrimidinic核酸内切酶,控制亲和力的DNA。

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摘要

Endonuclease IV (EndoIV) is an endonuclease that acts at apurinic/apyrimidinic (AP) sites and is classified as either long-type or short-type. The crystal structures of representative types of EndoIV from Geobacillus kaustophilus and Thermus thermophilus HB8 were determined using X-ray crystallography. G. kaustophilus EndoIV (the long type) had a higher affinity for double-stranded DNA containing an AP-site analogue than T. thermophilus EndoIV (the short type). Structural analysis of the two different EndoIVs suggested that a C-terminal DNA-recognition loop that is only present in the long type contributes to its high affinity for AP sites. A mutation analysis showed that Lys267 in the C-terminal DNA-recognition loop plays an important role in DNA binding.
机译：核酸内切酶IV (EndoIV)是一种酶徒apurinic / apyrimidinic(美联社)网站和分为长形或short-type。的晶体结构类型的代表从Geobacillus EndoIV kaustophilus和栖热菌属酸奶有助于HB8测定使用x射线晶体学。双链的类型)有较高的亲和力比T DNA包含AP-site模拟。酸奶有助于EndoIV(短类型)。分析两种不同EndoIVs建议那是,c端DNA-recognition循环只出现在长类型导致的高亲和力美联社网站。表明Lys267 c端DNA-recognition循环中发挥着重要作用DNA结合。

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