2Z7G

Crystal structure of adenosine deaminase ligated with EHNA

Summary for 2Z7G

• Entry DOI: 10.2210/pdb2z7g/pdb
• Descriptor: Adenosine deaminase, ZINC ION, (2S,3R)-3-(6-amino-9H-purin-9-yl)nonan-2-ol, ... (4 entities in total)
• Functional Keywords: beta barrel, protein-inhibitor complex, acetylation, hydrolase, nucleotide metabolism, pharmaceutical, polymorphism
• Biological source: Bos taurus (bovine)
• Cellular location: Cell membrane; Peripheral membrane protein; Extracellular side (By similarity): P56658
• Total number of polymer chains: 1
• Total formula weight: 40684.45

Authors

Kinoshita, T. (deposition date: 2007-08-20, release date: 2008-07-01, Last modification date: 2023-11-01)

Primary citation

Kinoshita, T.,Tada, T.,Nakanishi, I.
Conformational change of adenosine deaminase during ligand-exchange in a crystal
Biochem.Biophys.Res.Commun., 373:53-57, 2008

PubMed Abstract: Adenosine deaminase (ADA) perpetuates chronic inflammation by degrading extracellular adenosine which is toxic for lymphocytes. ADA has two distinct conformations: open form and closed form. From the crystal structures with various ligands, the non-nucleoside type inhibitors bind to the active site occupying the critical water-binding-position and sustain the open form of apo-ADA. In contrast, substrate mimics do not occupy the critical position, and induce the large conformational change to the closed form. However, it is difficult to predict the binding of (+)-erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA), as it possesses characteristic parts of both the substrate and the non-nucleoside inhibitors. The crystal structure shows that EHNA binds to the open form through a novel recognition of the adenine base accompanying conformational change from the closed form of the PR-ADA complex in crystalline state.

PubMed: 18549808
DOI: 10.1016/j.bbrc.2008.05.180

Experimental method

X-RAY DIFFRACTION (2.52 Å)