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透明质酸裂解酶的结构表明活性位点的打开/关闭状态与相邻环的构象之间存在相关性。

Structures of hyaluronate lyases suggest a correlation between active site opened/closed state and conformation of abutting loop.

作者信息

McNally Randall, Murali Ramachandran

机构信息

Department of Biomedical Sciences, Research Division of Immunology, Cedars-Sinai Medical Center, Los Angeles, California, United States.

出版信息

MicroPubl Biol. 2024 Jul 30;2024. doi: 10.17912/micropub.biology.001237. eCollection 2024.

DOI:10.17912/micropub.biology.001237
PMID:39144099
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11322831/
Abstract

The structures of hyaluronate lyases from two strains have been reported recently and show open catalytic clefts. We compared these open structures with more closed structures of homologous lyases and found that the conformation of a loop that abuts the catalytic cleft is seemingly correlated with the opening and closing of the cleft. We illustrate that the loop conformation seen in the open lyase appears incompatible with a closed catalytic cleft, and vice versa; however, mutations designed to disrupt the loop conformation did not significantly affect catalytic activity.

摘要

最近报道了来自两种菌株的透明质酸裂解酶的结构,这些结构显示出开放的催化裂隙。我们将这些开放结构与同源裂解酶更封闭的结构进行了比较,发现邻接催化裂隙的一个环的构象似乎与裂隙的开闭相关。我们证明,在开放裂解酶中看到的环构象似乎与封闭的催化裂隙不相容,反之亦然;然而,设计用于破坏环构象的突变并没有显著影响催化活性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ce7c/11322831/37d55625743b/25789430-2024-micropub.biology.001237.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ce7c/11322831/37d55625743b/25789430-2024-micropub.biology.001237.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ce7c/11322831/37d55625743b/25789430-2024-micropub.biology.001237.jpg

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