1B8J

ALKALINE PHOSPHATASE COMPLEXED WITH VANADATE

Summary for 1B8J

• Entry DOI: 10.2210/pdb1b8j/pdb
• Descriptor: PROTEIN (ALKALINE PHOSPHATASE), ZINC ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: alkaline phosphatase, hydrolase, phosphoric monoester, transferase (phospho, alcohol acceptor), vanadate
• Biological source: Escherichia coli
• Cellular location: Periplasm: P00634
• Total number of polymer chains: 2
• Total formula weight: 94921.04

Authors

Holtz, K.M.,Stec, B.,Kantrowitz, E.R. (deposition date: 1999-02-01, release date: 1999-02-18, Last modification date: 2024-10-16)

Primary citation

Holtz, K.M.,Stec, B.,Kantrowitz, E.R.
A model of the transition state in the alkaline phosphatase reaction.
J.Biol.Chem., 274:8351-8354, 1999

PubMed Abstract: A high resolution crystal structure of Escherichia coli alkaline phosphatase in the presence of vanadate has been refined to 1.9 A resolution. The vanadate ion takes on a trigonal bipyramidal geometry and is covalently bound by the active site serine nucleophile. A coordinated water molecule occupies the axial position opposite the serine nucleophile, whereas the equatorial oxygen atoms of the vanadate ion are stabilized by interactions with both Arg-166 and the zinc metal ions of the active site. This structural complex supports the in-line displacement mechanism of phosphomonoester hydrolysis by alkaline phosphatase and provides a model for the proposed transition state in the enzyme-catalyzed reaction.

PubMed: 10085061
DOI: 10.1074/jbc.274.13.8351

Experimental method

X-RAY DIFFRACTION (1.9 Å)