3RL5

Rat metallophosphodiesterase MPPED2 H67R Mutant

Summary for 3RL5

• Entry DOI: 10.2210/pdb3rl5/pdb
• Related: 2HY0 2HY1 2HYP 3IB7 3IB8 3RL3 3RL4
• Descriptor: Metallophosphoesterase MPPED2, CALCIUM ION, NITRATE ION, ... (5 entities in total)
• Functional Keywords: alpha-beta fold, metallophosphodiesterase, active site mutant, single nucleotide polymorphism, hydrolase
• Biological source: Rattus norvegicus (brown rat,rat,rats)
• Total number of polymer chains: 1
• Total formula weight: 33721.95

Authors

Podobnik, M.,Dermol, U. (deposition date: 2011-04-19, release date: 2011-08-10, Last modification date: 2024-02-28)

Primary citation

Dermol, U.,Janardan, V.,Tyagi, R.,Visweswariah, S.S.,Podobnik, M.
Unique utilization of a phosphoprotein phosphatase fold by a mammalian phosphodiesterase associated with WAGR syndrome.
J.Mol.Biol., 412:481-494, 2011

PubMed Abstract: Metallophosphoesterase-domain-containing protein 2 (MPPED2) is a highly evolutionarily conserved protein with orthologs found from worms to humans. The human MPPED2 gene is found in a region of chromosome 11 that is deleted in patients with WAGR (Wilms tumor, aniridia, genitourinary anomalies, and mental retardation) syndrome, and MPPED2 may function as a tumor suppressor. However, the precise cellular roles of MPPED2 are unknown, and its low phosphodiesterase activity suggests that substrate hydrolysis may not be its prime function. We present here the structures of MPPED2 and two mutants, which show that the poor activity of MPPED2 is not only a consequence of the substitution of an active-site histidine residue by glycine but also due to binding of AMP or GMP to the active site. This feature, enhanced by structural elements of the protein, allows MPPED2 to utilize the conserved phosphoprotein-phosphatase-like fold in a unique manner, ensuring that its enzymatic activity can be combined with a possible role as a scaffolding or adaptor protein.

PubMed: 21824479
DOI: 10.1016/j.jmb.2011.07.060

Experimental method

X-RAY DIFFRACTION (1.26 Å)