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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The DNA-binding domain of BenM reveals the structural basis for the recognition of a T-N11-A sequence motif by LysR-type transcriptional regulators
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The DNA-binding domain of BenM reveals the structural basis for the recognition of a T-N11-A sequence motif by LysR-type transcriptional regulators

机译：BenM揭示了dna结合域T-N11-A的识别结构依据由LysR-type转录序列基序监管机构

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摘要

LysR-type transcriptional regulators (LTTRs) play critical roles in metabolism and constitute the largest family of bacterial regulators. To understand protein-DNA interactions, atomic structures of the DNA-binding domain and linker-helix regions of a prototypical LTTR, BenM, were determined by X-ray crystallography. BenM structures with and without bound DNA reveal a set of highly conserved amino acids that interact directly with DNA bases. At the N-terminal end of the recognition helix (3) of a winged-helix-turn-helix DNA-binding motif, several residues create hydrophobic pockets (Pro30, Pro31 and Ser33). These pockets interact with the methyl groups of two thymines in the DNA-recognition motif and its complementary strand, T-N11-A. This motif usually includes some dyad symmetry, as exemplified by a sequence that binds two subunits of a BenM tetramer (ATAC-N7-GTAT). Gln29 forms hydrogen bonds to adenine in the first position of the recognition half-site (ATAC). Another hydrophobic pocket defined by Ala28, Pro30 and Pro31 interacts with the methyl group of thymine, complementary to the base at the third position of the half-site. Arg34 interacts with the complementary base of the 3′ position. Arg53, in the wing, provides AT-tract recognition in the minor groove. For DNA recognition, LTTRs use highly conserved interactions between amino acids and nucleotide bases as well as numerous less-conserved secondary interactions.
机译：LysR-type转录监管机构(LTTRs)在新陈代谢和构成了至关重要的作用最大的细菌的监管机构。理解protein-DNA相互作用,原子dna结合结构域和一个典型的LTTR linker-helix地区,BenM由x射线晶体学。有或没有绑定DNA揭示BenM结构一组高度保守的氨基酸直接与DNA碱基进行交互。氨基的螺旋(3)的认可winged-helix-turn-helix dna结合主题,几个残留创建疏水口袋(Pro30 Pro31和Ser33)。的两个胸腺嘧啶甲基DNA-recognition主题及其互补链,T-N11-A。双对称,以一个序列结合两个子单元的BenM四聚物(ATAC-N7-GTAT)。腺嘌呤在第一位置的识别half-site (ATAC)。定义为Ala28, Pro30 Pro31交互胸腺嘧啶的甲基,互补的基地第三half-site的位置。Arg34互补碱基的相互作用3 '的位置。在小沟AT-tract识别。识别,LTTRs使用高度保守的氨基酸和核苷酸之间的相互作用基地以及众多less-conserved二次交互。

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