1TJ7

Structure determination and refinement at 2.44 A resolution of Argininosuccinate lyase from E. coli

Summary for 1TJ7

• Entry DOI: 10.2210/pdb1tj7/pdb
• Descriptor: Argininosuccinate lyase, PHOSPHATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: argininosuccinate lyase, crystallin, e. coli, fumarase, aspartase, lyase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P11447
• Total number of polymer chains: 2
• Total formula weight: 101214.33

Authors

Bhaumik, P.,Koski, M.K.,Bergman, U.,Wierenga, R.K. (deposition date: 2004-06-03, release date: 2004-10-26, Last modification date: 2023-08-23)

Primary citation

Bhaumik, P.,Koski, M.K.,Bergmann, U.,Wierenga, R.K.
Structure determination and refinement at 2.44 A resolution of argininosuccinate lyase from Escherichia coli.
Acta Crystallogr.,Sect.D, 60:1964-1970, 2004

PubMed Abstract: 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.

PubMed: 15502303
DOI: 10.1107/S0907444904021912

Experimental method

X-RAY DIFFRACTION (2.44 Å)