7D2F

Lp major histidine acid phosphatase mutant D281A/5'-AMP

Summary for 7D2F

• Entry DOI: 10.2210/pdb7d2f/pdb
• Descriptor: Major acid phosphatase, ADENOSINE MONOPHOSPHATE (3 entities in total)
• Functional Keywords: complex, 5'-amp, hydrolase
• Biological source: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
• Total number of polymer chains: 2
• Total formula weight: 74283.70

Authors

Guo, Y.,Teng, Y. (deposition date: 2020-09-16, release date: 2021-09-22, Last modification date: 2024-11-13)

Primary citation

Guo, Y.,Zhou, D.,Zhang, H.,Zhang, N.N.,Qi, X.,Chen, X.,Chen, Q.,Li, J.,Ge, H.,Teng, Y.B.
Structural insights into a new substrate binding mode of a histidine acid phosphatase from Legionella pneumophila.
Biochem.Biophys.Res.Commun., 540:90-94, 2021

PubMed Abstract: 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 mutant in complex with 5'-AMP were solved at 2.2 and 2.6 Å resolution, respectively. The structure of the MapA/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.

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)