Structures of Cutibacterium acnes hyaluronate lyases suggest a correlation between active site opened/closed state and conformation of abutting loop.
| Autor: | McNally R; Department of Biomedical Sciences, Research Division of Immunology, Cedars-Sinai Medical Center, Los Angeles, California, United States., Murali R; Department of Biomedical Sciences, Research Division of Immunology, Cedars-Sinai Medical Center, Los Angeles, California, United States. |
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| Jazyk: | angličtina |
| Zdroj: | MicroPublication biology [MicroPubl Biol] 2024 Jul 30; Vol. 2024. Date of Electronic Publication: 2024 Jul 30 (Print Publication: 2024). |
| DOI: | 10.17912/micropub.biology.001237 |
| Abstrakt: | The structures of hyaluronate lyases from two Cutibacterium acnes 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. Competing Interests: The authors declare that there are no conflicts of interest present. (Copyright: © 2024 by the authors.) |
| Databáze: | MEDLINE |
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