4pga
From Proteopedia
|
GLUTAMINASE-ASPARAGINASE FROM PSEUDOMONAS 7A
Overview
Pseudomonas 7A glutaminase-asparaginase (PGA) catalyzes the hydrolysis of, D- and L-isomers of glutamine and asparagine. X-ray quality type-1, crystals of PGA have been obtained from 2.0 M ammonium sulfate. The space, group is C222(1) with unit-cell dimensions a = 78.62, b = 135.80, and c =, 137.88 A. The tetrameric molecule is located on a crystallographic 2-fold, axis, and two subunits form the asymmetric portion of the unit cell. The, structure was solved by the molecular replacement method and refined at, 1.7 A resolution to an R = 19.9% with a good geometry of the model, G =, 0.05. The resultant electron density maps enabled us to resolve individual, constituent atoms of most residues and introduce minor revisions to the, amino acid sequence. The catalytic loop, Thr20-Gly40, is in ... [(full description)]
About this Structure
4PGA is a [Single protein] structure of sequence from [Pseudomonas sp. 7a] with SO4 and NH4 as [ligands]. Active as [[1]], with EC number [3.5.1.38]. Full crystallographic information is available from [OCA].
Reference
Ion binding induces closed conformation in Pseudomonas 7A glutaminase-asparaginase (PGA): crystal structure of the PGA-SO4(2-)-NH4+ complex at 1.7 A resolution., Jakob CG, Lewinski K, LaCount MW, Roberts J, Lebioda L, Biochemistry. 1997 Jan 28;36(4):923-31. PMID:9020792
Page seeded by OCA on Mon Oct 29 16:57:11 2007
