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Structural insights into a new substrate binding mode of a histidine acid phosphatase from Legionella pneumophila.

Biochemical and biophysical research communications - 12 Feb 2021

Guo Yu, Zhou Dan, Zhang Hui, Zhang Nan-Nan, Qi Xiaoyu, Chen Xiaofang, Chen Qi, Li Jing, Ge Honghua, Teng Yan-Bin

Abstract excerpt

MapA is a histidine acid phosphatase (HAP) from Legionella pneumophila that catalyzes the hydroxylation of a phosphoryl group from phosphomonoesters by an active-site histidine. Several structures of HAPs, including MapA, in complex with the inhibitor tartrate have been solved and the substrate binding tunnel identified; however, the substrate recognition mechanism remains unknown. To gain insight into the...

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Identifiers

PMID: 33450485
DOI: 10.1016/j.bbrc.2020.12.070

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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