3DYL

human phosphdiesterase 9 substrate complex (ES complex)

Summary for 3DYL

• Entry DOI: 10.2210/pdb3dyl/pdb
• Related: 3DY8 3DYN 3DYQ 3DYS
• Descriptor: human phosphodiesterase 9, MANGANESE (II) ION, MAGNESIUM ION, ... (7 entities in total)
• Functional Keywords: phosphodiesterase, enzyme mechanism, cgmp, hydrolase, manganese, metal-binding, phosphoprotein
• Biological source: Homo sapiens (Human)
• Cellular location: Isoform PDE9A1: Cell projection, ruffle membrane. Isoform PDE9A2: Cell projection, ruffle membrane. Isoform PDE9A3: Cytoplasm. Isoform PDE9A17: Cytoplasm: O76083
• Total number of polymer chains: 2
• Total formula weight: 78497.81

Authors

Liu, S.,Mansour, M.N.,Dillman, K.,Perez, J.,Danley, D.,Menniti, F. (deposition date: 2008-07-28, release date: 2008-09-16, Last modification date: 2024-02-21)

Primary citation

Liu, S.,Mansour, M.N.,Dillman, K.S.,Perez, J.R.,Danley, D.E.,Aeed, P.A.,Simons, S.P.,Lemotte, P.K.,Menniti, F.S.
Structural basis for the catalytic mechanism of human phosphodiesterase 9.
Proc.Natl.Acad.Sci.Usa, 105:13309-13314, 2008

PubMed Abstract: The phosphodiesterases (PDEs) are metal ion-dependent enzymes that regulate cellular signaling by metabolic inactivation of the ubiquitous second messengers cAMP and cGMP. In this role, the PDEs are involved in many biological and metabolic processes and are proven targets of successful drugs for the treatments of a wide range of diseases. However, because of the rapidity of the hydrolysis reaction, an experimental knowledge of the enzymatic mechanisms of the PDEs at the atomic level is still lacking. Here, we report the structures of reaction intermediates accumulated at the reaction steady state in PDE9/crystal and preserved by freeze-trapping. These structures reveal the catalytic process of a PDE and explain the substrate specificity of PDE9 in an actual reaction and the cation requirements of PDEs in general.

PubMed: 18757755
DOI: 10.1073/pnas.0708850105

Experimental method

X-RAY DIFFRACTION (2.7 Å)