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首页> 外文期刊>Acta crystallographica. Section D, Structural biology >Structural and biochemical analyses of the tetrameric carboxypeptidase S9Cfn from Fusobacterium nucleatum
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Structural and biochemical analyses of the tetrameric carboxypeptidase S9Cfn from Fusobacterium nucleatum

机译：结构和生化分析四聚物的羧肽酶S9Cfn从梭菌属nucleatum

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摘要

As one of the most abundant bacteria in the human oral cavity, Fusobacterium nucleatum is closely involved in various oral diseases and is also a risk factor for other diseases. The peptidases of F. nucleatum can digest exogenous peptides into amino acids to satisfy its nutrient requirements. Here, a putative F. nucleatum peptidase, termed S9Cfn, which belongs to the S9C peptidase family was identified. Enzymatic activity assays combined with mass-spectrometric analysis revealed that S9Cfn is a carboxypeptidase, but not an aminopeptidase as previously annotated. The crystal structure of the S9Cfn tetramer was solved at 2.6?? resolution and was found to contain a pair of oligomeric pores in the center. Structural analysis, together with site-directed mutagenesis and enzymatic activity assays, revealed a substrate-entrance tunnel that extends from each oligomeric pore to the catalytic triad, adjacent to which three conserved arginine residues are responsible for substrate binding. Moreover, comparison with other S9 peptidase structures indicated drastic conformational changes of the oligomeric pores during the catalytic cycle. Together, these findings increase the knowledge of this unique type of tetrameric carboxypeptidase and provide insight into the homeostatic control of microbiota in the human oral cavity.
机译：作为一个在人类最丰富的细菌口腔、梭菌属nucleatum密切参与各种口腔疾病和也是一个其他疾病的危险因素。f . nucleatum能消化外源肽氨基酸来满足营养需求。在这里,一个假定的f . nucleatum肽酶,称为S9Cfn,属于S9C肽酶家族被确认。结合质谱分析透露,S9Cfn羧肽酶,但是不像以前带注释的一个氨基肽酶。的晶体结构S9Cfn四聚物解决了在2.6 ? ?包含一对寡聚孔的中心。结构分析和定点酶活性测定诱变和揭示了substrate-entrance隧道扩展从每个毛孔低聚物的催化三分子,相邻的三个守恒的精氨酸残留负责衬底绑定。此外,比较与其他S9肽酶结构表明激烈的构象变化的低聚物的毛孔中催化循环。增加这一独特的类型的知识四聚物的羧肽酶,并提供洞察力进入稳态控制的微生物群人类的口腔。

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