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Structural insights into caspase ADPR-deacylization catalyzed by a bacterial effector and host calmodulin

ABSTRACT: identification of CopC-catalyzed ADPR-deacylization modification site of caspase-3/-7/-8/-9

ORGANISM(S): Homo Sapiens

SUBMITTER: Shan Li

PROVIDER: PXD035969 | iProX | Wed Aug 10 00:00:00 BST 2022

REPOSITORIES: iProX

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Structural insights into caspase ADPR deacylization catalyzed by a bacterial effector and host calmodulin.

Zhang Kuo K Peng Ting T Tao Xinyuan X Tian Miao M Li Yanxin Y Wang Zhao Z Ma Shuaifei S Hu Shufan S Pan Xing X Xue Juan J Luo Jiwei J Wu Qiulan Q Fu Yang Y Li Shan S

Molecular cell 20221123 24

Programmed cell death and caspase proteins play a pivotal role in host innate immune response combating pathogen infections. Blocking cell death is employed by many bacterial pathogens as a universal virulence strategy. CopC family type III effectors, including CopC from an environmental pathogen Chromobacterium violaceum, utilize calmodulin (CaM) as a co-factor to inactivate caspases by arginine ADPR deacylization. However, the molecular basis of the catalytic and substrate/co-factor binding me ...[more]

PMID: 36423631

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