2DKB

DIALKYLGLYCINE DECARBOXYLASE STRUCTURE: BIFUNCTIONAL ACTIVE SITE AND ALKALI METAL BINDING SITES

Summary for 2DKB

• Entry DOI: 10.2210/pdb2dkb/pdb
• Descriptor: 2,2-DIALKYLGLYCINE DECARBOXYLASE (PYRUVATE), SODIUM ION, PYRIDOXAL-5'-PHOSPHATE, ... (5 entities in total)
• Functional Keywords: lyase(decarboxylase)
• Biological source: Burkholderia cepacia
• Total number of polymer chains: 1
• Total formula weight: 47065.76

Authors

Toney, M.D.,Hohenester, E.,Jansonius, J.N. (deposition date: 1994-07-12, release date: 1994-10-15, Last modification date: 2017-11-29)

Primary citation

Toney, M.D.,Hohenester, E.,Cowan, S.W.,Jansonius, J.N.
Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites.
Science, 261:756-759, 1993

PubMed Abstract: The structure of the bifunctional, pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase was determined to 2.1-angstrom resolution. Model building suggests that a single cleavage site catalyzes both decarboxylation and transamination by maximizing stereoelectronic advantages and providing electrostatic and general base catalysis. The enzyme contains two binding sites for alkali metal ions. One is located near the active site and accounts for the dependence of activity on potassium ions. The other is located at the carboxyl terminus of an alpha helix. These sites help show how proteins can specifically bind alkali metals and how these ions can exert functional effects.

PubMed: 8342040

Experimental method

X-RAY DIFFRACTION (2.1 Å)