Structure of recombinant prolidase fromThermococcus sibiricusin space groupP21221

Abstract

The crystal structure of recombinant prolidase fromThermococcus sibiricuswas 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 groupP21221, with unit-cell parametersa= 97.60,b= 123.72,c= 136.52 Å, α = β = γ = 90°. The structure was refined to anRcrystof 22.1% and anRfreeof 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.