1tj7
From Proteopedia
Structure determination and refinement at 2.44 A resolution of Argininosuccinate lyase from E. coli
Overview
Escherichia coli argininosuccinate lyase has been crystallized from a highly concentrated sample of purified recombinant alpha-methylacyl-CoA racemase, in which it occurred as a minor impurity. The structure has been solved using molecular replacement at 2.44 A resolution. The enzyme is tetrameric, but in this crystal form there is a dimer in the asymmetric unit. The tetramer has four active sites; each active site is constructed from loops of three different subunits. One of these catalytic loops, near residues Ser277 and Ser278, was disordered in previous structures of active lyases, but is very well ordered in this structure in one of the subunits owing to the presence of two phosphate ions in the active-site cavity. The positions of these phosphate ions indicate a plausible mode of binding of the succinate moiety of the substrate in the competent catalytic complex.
About this Structure
1TJ7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure determination and refinement at 2.44 A resolution of argininosuccinate lyase from Escherichia coli., Bhaumik P, Koski MK, Bergmann U, Wierenga RK, Acta Crystallogr D Biol Crystallogr. 2004 Nov;60(Pt 11):1964-70. Epub 2004, Oct 20. PMID:15502303 Page seeded by OCA on Sat May 3 10:00:41 2008
