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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structural characterization of a modification subunit of a putative type i restriction enzyme from Vibrio vulnificus YJ016
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Structural characterization of a modification subunit of a putative type i restriction enzyme from Vibrio vulnificus YJ016

机译:结构描述的修改亚基的假定的i型限制性内切酶从创伤弧菌YJ016

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摘要

In multifunctional type I restriction enzymes, active methyltransferases (MTases) are constituted of methylation (HsdM) and specificity (HsdS) subunits. In this study, the crystal structure of a putative HsdM subunit from Vibrio vulnificus YJ016 (vvHsdM) was elucidated at a resolution of 1.80 ?. A cofactor-binding site for S-adenosyl-l-methionine (SAM, a methyl-group donor) is formed within the C-terminal domain of an/Β-fold, in which a number of residues are conserved, including the GxGG and (N/D)PP(F/Y) motifs, which are likely to interact with several functional moieties of the SAM methyl-group donor. Comparison with the N6 DNA MTase of Thermus aquaticus and other HsdM structures suggests that two aromatic rings (Phe199 and Phe312) in the motifs that are conserved among the HsdMs may sandwich both sides of the adenine ring of the recognition sequence so that a conserved Asn residue (Asn309) can interact with the N6 atom of the target adenine base (a methyl-group acceptor) and locate the target adenine base close to the transferred SAM methyl group.
机译:在多功能I型限制性内切酶,活跃的甲基转移酶(mta协同工作)构成的甲基化(HsdM)和特异性(hsd)子单元。从弧菌假定的HsdM亚基的结构本文描述YJ016 (vvHsdM)被阐明解决1.80 ?。S-adenosyl-l-methionine(山姆,甲基捐赠)的c端域内形成的an /Β倍,大量的残留守恒的,包括GxGG和(N / D) PP (F / Y)图案,这可能与几个交互功能的半个山姆甲基捐献者。水生栖热菌和其他HsdM结构表明两个芳香环(Phe199和Phe312)的主题是守恒的双方的腺嘌呤HsdMs可能三明治环的识别序列这一个守恒的Asn残渣(Asn309)可以与之交互目标的N6原子(腺嘌呤基地甲基受体)和定位目标腺嘌呤基接近山姆甲基转移组。

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