7doq

Publication Abstract from PubMed

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 mechanism of substrate recognition, the crystal structures of apo-MapA and the MapA(D281A) mutant in complex with 5'-AMP were solved at 2.2 and 2.6 A resolution, respectively. The structure of the MapA(D281A)/5'-AMP complex reveals that the 5'-AMP fits fully into the substrate binding tunnel, with the 2'-hydroxyl group of the ribose moiety stabilized by Glu201 and the adenine moiety sandwiched between His205 and Phe237. This is the second structure of a HAP/AMP complex solved with 5'-AMP binding in a unique manner in the active site. The structure presents a new substrate recognition mechanism of HAPs.

Structural insights into a new substrate binding mode of a histidine acid phosphatase from Legionella pneumophila.,Guo Y, Zhou D, Zhang H, Zhang NN, Qi X, Chen X, Chen Q, Li J, Ge H, Teng YB Biochem Biophys Res Commun. 2021 Feb 12;540:90-94. doi:, 10.1016/j.bbrc.2020.12.070. Epub 2021 Jan 12. PMID:33450485^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.