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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of MrsD, an FAD-binding protein of the HFCD family.
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Structure of MrsD, an FAD-binding protein of the HFCD family.

机译：MrsD结构,一个FAD-binding蛋白质的HFCD家庭。

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摘要

MrsD from Bacillus sp. HIL-Y85/54728 is a member of the HFCD (homo-oligomeric flavin-containing Cys decarboxylases) family of flavoproteins and is involved in the biosynthesis of the lantibiotic mersacidin. It catalyses the oxidative decarboxylation of the C-terminal cysteine residue of the MrsA precursor peptide of mersacidin, yielding a (Z)-enethiol intermediate as the first step in the formation of the unusual amino acid S-[(Z)-2-aminovinyl]-methyl-D-cysteine. Surprisingly, MrsD was found to bind FAD, in contrast to the three other characterized members of the HFCD family, which bind FMN. To determine the molecular discriminators of FAD binding within the HFCD family, the crystal structure of MrsD was analyzed at a resolution of 2.54 A. Crystals of space group F432 contain one MrsD monomer in the asymmetric unit. However, a Patterson search with EpiD-derived models failed. Based on the consideration that the dodecameric MrsD particle of tetrahedral symmetry resembles the quaternary structure of EpiD, rotational and translational parameters were derived from the geometric consideration that the MrsD dodecamer is generated from a monomer by crystallographic symmetry around the position (1/4, 1/4, 1/4) of the unit cell. A structural comparison with the FMN-binding members of the HFCD family EpiD and AtHAL3a shows conserved sequence motifs in contact with the flavin's pyrimidine ring but divergent environments for the dimethylbenzene ring of the isoalloxazine moiety. The position of the ribityl chain differs in MrsD from that found in EpiD and AtHAL3a. However, the FMN-phosphate binding sites are also highly conserved in their exact positions. In all three cases, the flavin cofactor is bound to a structurally conserved region of the Rossmann-fold monomer, exposing its Re side for catalysis. The adenosyl phosphate of FAD is anchored in a well defined binding site and the adenosine moieties are oriented towards the interior of the hollow particle, where three of them pack against each other around the threefold axis of a trimeric facet.
机译：从芽孢杆菌sp MrsD。HIL-Y85/54728是一个成员HFCD (homo-oligomeric flavin-containing黄素蛋白家族和半胱氨酸脱羧酶)参与生物合成的lantibiotic mersacidin。氧化脱羧的c端耐甲氧西林金黄色葡萄球菌前体肽的半胱氨酸残基mersacidin,收益率(Z) -enethiol中间的不寻常的形成的第一步氨基酸S - (Z) 2-aminovinyl -methyl-D-cysteine。令人惊讶的是,MrsD发现结合时尚,与其他三个成员绑定FMN HFCD家族的。时尚的分子鉴别器绑定HFCD家庭内的晶体结构2.54 MrsD的分辨率进行了分析。晶体的空间群F432包含一个MrsD单体的不对称单元。帕特森与EpiD-derived模型搜索失败了。基于dodecameric的考虑MrsD粒子的四面体对称相似EpiD的四级结构,转动是由平移参数几何考虑,MrsD dodecamer从单体通过晶体生成对称的位置(1/4,1/4,1/4)单位细胞。FMN-binding HFCD家庭EpiD的成员AtHAL3a显示保守序列图案与黄素的嘧啶环但接触不同环境对二甲苯异咯嗪环的一部分。从发现ribityl链在MrsD有所不同EpiD AtHAL3a。在他们的结合位点也高度保守的确切的位置。代数余子式绑定到结构守恒的Rossmann-fold单体的地区,暴露自己的催化。时尚是固定在一个定义良好的结合位点腺苷是面向半个空心粒子的内部,三人他们相互包的三轴三聚物的方面。

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