4BKM

Crystal structure of the murine AUM (phosphoglycolate phosphatase) capping domain as a fusion protein with the catalytic core domain of murine chronophin (pyridoxal phosphate phosphatase)

Summary for 4BKM

• Entry DOI: 10.2210/pdb4bkm/pdb
• Descriptor: PYRIDOXAL PHOSPHATE PHOSPHATASE, PHOSPHOGLYCOLATE PHOSPHATASE, PYRIDOXAL PHOSPHATE PHOSPHATASE, MAGNESIUM ION, NITRATE ION, ... (4 entities in total)
• Functional Keywords: had family, hydrolase
• Biological source: MUS MUSCULUS (HOUSE MOUSE); More
• Cellular location: Cytoplasm, cytosol : P60487
• Total number of polymer chains: 4
• Total formula weight: 134070.93

Authors

Knobloch, G.,Seifried, A.,Gohla, A.,Schindelin, H. (deposition date: 2013-04-26, release date: 2013-12-25, Last modification date: 2024-10-09)

Primary citation

Seifried, A.,Knobloch, G.,Duraphe, P.S.,Segerer, G.,Manhard, J.,Schindelin, H.,Schultz, J.,Gohla, A.
Evolutionary and Structural Analyses of the Mammalian Haloacid Dehalogenase-Type Phosphatases Aum and Chronophin Provide Insight Into the Basis of Their Different Substrate Specificities.
J.Biol.Chem., 289:3416-, 2014

PubMed Abstract: Mammalian haloacid dehalogenase (HAD)-type phosphatases are an emerging family of phosphatases with important functions in physiology and disease, yet little is known about the basis of their substrate specificity. Here, we characterize a previously unexplored HAD family member (gene annotation, phosphoglycolate phosphatase), which we termed AUM, for aspartate-based, ubiquitous, Mg(2+)-dependent phosphatase. AUM is a tyrosine-specific paralog of the serine/threonine-specific protein and pyridoxal 5'-phosphate-directed HAD phosphatase chronophin. Comparative evolutionary and biochemical analyses reveal that a single, differently conserved residue in the cap domain of either AUM or chronophin is crucial for phosphatase specificity. We have solved the x-ray crystal structure of the AUM cap fused to the catalytic core of chronophin to 2.65 Å resolution and present a detailed view of the catalytic clefts of AUM and chronophin that explains their substrate preferences. Our findings identify a small number of cap domain residues that encode the different substrate specificities of AUM and chronophin.

PubMed: 24338473
DOI: 10.1074/JBC.M113.503359

Experimental method

X-RAY DIFFRACTION (2.65 Å)