title: Structure of recombinant prolidase from Thermococcus sibiricus in space group P21221.
abstract: The crystal structure of recombinant prolidase from Thermococcus sibiricus was determined by X-ray diffraction at a resolution of 2.6 Å and was found to contain a tetramer in the asymmetric unit. A protein crystal grown in microgravity using the counter-diffusion method was used for X-ray studies. The crystal belonged to space group P21221, with unit-cell parameters a = 97.60, b = 123.72, c = 136.52 Å, α = β = γ = 90°. The structure was refined to an Rcryst of 22.1% and an Rfree of 29.6%. The structure revealed flexible folding of the N-terminal domain of the protein as well as high variability in the positions of the bound metal ions. The coordinates of the resulting model were deposited in the Protein Data Bank as entry 4rgz.
authors.affiliation: Protein Factory, National Research Centre `Kurchatov Institute', Akademika Kurchatova Square 1, Moscow 123182, Russian Federation.
authors.forename: Vladimir
authors.initials: V
authors.lastname: Timofeev
authors.affiliation: Laboratory of Enzyme Engineering, Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii Prospekt 33, Moscow 119071, Russian Federation.
authors.forename: Elvira
authors.initials: E
authors.lastname: Slutskaya
authors.affiliation: Protein Factory, National Research Centre `Kurchatov Institute', Akademika Kurchatova Square 1, Moscow 123182, Russian Federation.
authors.forename: Marina
authors.initials: M
authors.lastname: Gorbacheva
authors.affiliation: Protein Factory, National Research Centre `Kurchatov Institute', Akademika Kurchatova Square 1, Moscow 123182, Russian Federation.
authors.forename: Konstantin
authors.initials: K
authors.lastname: Boyko
authors.affiliation: Protein Factory, National Research Centre `Kurchatov Institute', Akademika Kurchatova Square 1, Moscow 123182, Russian Federation.
authors.forename: Tatiana
authors.initials: T
authors.lastname: Rakitina
authors.affiliation: Protein Factory, National Research Centre `Kurchatov Institute', Akademika Kurchatova Square 1, Moscow 123182, Russian Federation.
authors.forename: Dmitry
authors.initials: D
authors.lastname: Korzhenevskiy
authors.affiliation: Protein Factory, National Research Centre `Kurchatov Institute', Akademika Kurchatova Square 1, Moscow 123182, Russian Federation.
authors.forename: Alexey
authors.initials: A
authors.lastname: Lipkin
authors.affiliation: Protein Factory, National Research Centre `Kurchatov Institute', Akademika Kurchatova Square 1, Moscow 123182, Russian Federation.
authors.forename: Vladimir
authors.initials: V
authors.lastname: Popov
mesh_terms: D020816:Amino Acid Motifs; D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004150:Dipeptidases / Q000737:chemistry* / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017510:Protein Folding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D019712:Thermococcus / Q000737:chemistry* / Q000201:enzymology
chemical_list: D019843:Archaeal Proteins; D011994:Recombinant Proteins; D004150:Dipeptidases; C022449:proline dipeptidase
keywords: Thermococcus sibiricus; archaeal proteins; crystallization; crystallography; prolidase