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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >Selecting soluble/foldable protein domains through single-gene or genomic ORF filtering: structure of the head domain of Burkholderia pseudomallei antigen BPSL2063
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Selecting soluble/foldable protein domains through single-gene or genomic ORF filtering: structure of the head domain of Burkholderia pseudomallei antigen BPSL2063

机译：通过选择溶性/可折叠蛋白质域单基因或基因组ORF过滤:结构洋葱头域的举办抗原BPSL2063

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摘要

The 1.8 angstrom resolution crystal structure of a conserved domain of the potential Burkholderia pseudomallei antigen and trimeric autotransporter BPSL2063 is presented as a structural vaccinology target for melioidosis vaccine development. Since BPSL2063 (1090 amino acids) hosts only one conserved domain, and the expression/purification of the full-length protein proved to be problematic, a domain-filtering library was generated using beta-lactamase as a reporter gene to select further BPSL2063 domains. As a result, two domains (D1 and D2) were identified and produced in soluble form in Escherichia coli. Furthermore, as a general tool, a genomic open reading frame-filtering library from the B. pseudomallei genome was also constructed to facilitate the selection of domain boundaries from the entire ORFeome. Such an approach allowed the selection of three potential protein antigens that were also produced in soluble form. The results imply the further development of ORF-filtering methods as a tool in protein-based research to improve the selection and production of soluble proteins or domains for downstream applications such as X-ray crystallography.
机译：1.8埃分辨率晶体结构守恒的领域潜在的洋葱举办抗原和三聚物的autotransporterBPSL2063呈现结构性疫苗学类鼻疽疫苗开发的目标。BPSL2063(1090个氨基酸)主机只有一个守恒的域,表达式/净化完整的蛋白质了问题,domain-filtering库使用beta-lactamase生成作为报告基因进一步选择BPSL2063域。两个域(D1和D2)和识别在大肠杆菌产生的可溶性形式。此外,作为一个通用的工具,一个基因开放阅读图书馆从B帧过滤。举办基因组也建造方便的选择域边界从整个ORFeome。三个潜在的选择蛋白质抗原这也产生了以可溶性形式。结果意味着的进一步发展在蛋白质ORF-filtering方法作为一种工具研究提高选择和生产为下游的可溶性蛋白质或域应用x射线晶体学等。

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