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Confirmation of the binding site of spermine to ATP13A2 protein

ABSTRACT: To better understand human ATP13A2-mediated polyamine transport, we used single-particle cryo-electron microscopy to solve high-resolution structures of human ATP13A2. Interestingly, we found polyamine binding at multiple sites distributed along the transmembrane regions in ATP13A2 protein, which has not been reported in previous studies. Therefore, we used cross-linking mass spectrometry (CX-MS) to confirm potential binding sites.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: jianqiang Mu

LAB HEAD: Zhongmin LIU

PROVIDER: PXD037493 | Pride | 2023-05-10

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	ATP13A2-WT_Crosslink.csv	Csv
	ATP13A2-WT_Looplink.csv	Csv
	ATP13A2-WT_Monolink.csv	Csv
	ATP13A2-WT_SPM.csv	Csv
	ATP13A2_Q9NQ11-1_.fasta	Fasta

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Publications

Conformational cycle of human polyamine transporter ATP13A2.

Mu Jianqiang J Xue Chenyang C Fu Lei L Yu Zongjun Z Nie Minhan M Wu Mengqi M Chen Xinmeng X Liu Kun K Bu Ruiqian R Huang Ying Y Yang Baisheng B Han Jianming J Jiang Qianru Q Chan Kevin C KC Zhou Ruhong R Li Huilin H Huang Ancheng A Wang Yong Y Liu Zhongmin Z

Nature communications 20230408 1

Dysregulation of polyamine homeostasis strongly associates with human diseases. ATP13A2, which is mutated in juvenile-onset Parkinson's disease and autosomal recessive spastic paraplegia 78, is a transporter with a critical role in balancing the polyamine concentration between the lysosome and the cytosol. Here, to better understand human ATP13A2-mediated polyamine transport, we use single-particle cryo-electron microscopy to solve high-resolution structures of human ATP13A2 in six intermediate ...[more]

PMID: 37031211

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Project description:The mass spectrometry data of a previous publication (Chen et.al. 2009 doi:10.1038/emboj.2009.401) were reprocesed and is used for method developing, teaching and training purpose.

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Integrative structure models of the α-Synuclein dimer conformations

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Characterizing protein conformers by cross-linking mass spectrometry and pattern recognition

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