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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of internalin C from Listeria monocytogenes
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Structure of internalin C from Listeria monocytogenes

机译：从李斯特菌internalin C的结构monocytogenes

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摘要

The crystal structure of internalin C (InlC) from Listeria monocytogenes has been determined at 2.0 angstrom resolution. Several observations implicate InlC in infection: inlC has the same transcriptional activator as other virulence genes, it is only present in pathogenic Listeria strains and an inlC deletion mutant is significantly less virulent. While the extended concave receptor-binding surfaces of the leucine-rich repeat (LRR) domains of internalins A and B have aromatic clusters involved in receptor binding, the corresponding surface of InlC is smaller, flatter and more hydrophilic, suggesting that InlC may be involved in weak or transient associations with receptors; this may help explain why no receptor has yet been discovered for InlC. In contrast, the Ig- like domain, to which the LRR domain is fused, has surface aromatics that may be of functional importance, possibly being involved in binding to the surface of the bacteria or in receptor binding.
机译：internalin C (InlC)的晶体结构单核细胞增多性李斯特氏菌已被确定为2.0埃分辨率。暗示InlC感染:InlC相同转录激活其他毒性基因,只有出现在致病性李斯特菌菌株和inlC缺失突变体更少的毒性。凹的表面受体结合internalins富亮氨酸重复(远程雷达)领域A和B芳香集群参与受体结合,相应的表面InlC比较小,奉承更亲水,表明InlC可能参与或疲软瞬态关联与受体;有助于解释为什么受体尚未发现InlC。域,远程雷达领域的融合,表面芳烃功能的重要性,可能参与绑定表面的细菌或受体绑定。

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