3CZ4

Native AphA class B acid phosphatase/phosphotransferase from E. coli

Summary for 3CZ4

• Entry DOI: 10.2210/pdb3cz4/pdb
• Related: 1n8n 1n9k 1rmq 1rmy 2g1a 2hf7
• Descriptor: Class B acid phosphatase, MAGNESIUM ION, ACETATE ION, ... (6 entities in total)
• Functional Keywords: hydrolase, acid phosphatase/phosphotransferase, metallo phosphatase, magnesium, metal-binding, periplasm
• Biological source: Escherichia coli
• Cellular location: Periplasm (Potential): P0AE22
• Total number of polymer chains: 1
• Total formula weight: 24008.79

Authors

Leone, R.,Cappelletti, E.,Benvenuti, M.,Lentini, G.,Thaller, M.C.,Mangani, S. (deposition date: 2008-04-28, release date: 2008-11-11, Last modification date: 2023-08-30)

Primary citation

Leone, R.,Cappelletti, E.,Benvenuti, M.,Lentini, G.,Thaller, M.C.,Mangani, S.
Structural insights into the catalytic mechanism of the bacterial class B phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases.
J.Mol.Biol., 384:478-488, 2008

PubMed Abstract: AphA is a magnesium-dependent, bacterial class B acid phosphatase that catalyzes the hydrolysis of a variety of phosphoester substrates and belongs to the DDDD superfamily of phosphohydrolases. The recently reported crystal structure of AphA from Escherichia coli has revealed the quaternary structure of the enzyme together with hints about its catalytic mechanism. The present work reports the crystal structures of AphA from E. coli in complex with substrate, transition-state, and intermediate analogues. The structures provide new insights into the mechanism of the enzyme and allow a revision of some aspects of the previously proposed mechanism that have broader implications for all the phosphatases of the DDDD superfamily.

PubMed: 18845157
DOI: 10.1016/j.jmb.2008.09.050

Experimental method

X-RAY DIFFRACTION (1.7 Å)