Dabin Jérôme, Jam Murielle, Czjzek Mirjam, Michel Gurvan
UPMC University Paris 06, UMR 7139, Marine Plants and Biomolecules, Station Biologique de Roscoff, F-29682 Roscoff, Bretagne, France.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Mar 1;64(Pt 3):224-7. doi: 10.1107/S1744309108004387. Epub 2008 Feb 29.
Polysaccharide lyases belonging to family PL1 act on pectins. These anionic polymers are usually produced by terrestrial plants and therefore pectinolytic enzymes are not frequently observed in marine microorganisms. The protein RB5312 from the marine bacterium Rhodopirellula baltica is distantly related to family PL1 pectate lyases, but its exact function is unclear. In this study, the expression and purification of a recombinant form of RB5312 are described. This protein was crystallized using the hanging-drop vapour-diffusion method. The crystals belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 39.05, b = 144.05, c = 153.97 A, alpha = beta = gamma = 90 degrees. A complete data set was collected to 1.8 A resolution from a native crystal.
属于PL1家族的多糖裂解酶作用于果胶。这些阴离子聚合物通常由陆生植物产生，因此在海洋微生物中不常观察到果胶分解酶。来自海洋细菌波罗的海玫瑰单胞菌的蛋白质RB5312与PL1家族果胶酸裂解酶的亲缘关系较远，但其确切功能尚不清楚。在本研究中，描述了重组形式的RB5312的表达和纯化。该蛋白质采用悬滴气相扩散法结晶。晶体属于空间群P2(1)2(1)2(1)，晶胞参数a = 39.05，b = 144.05，c = 153.97 Å，α = β = γ = 90°。从天然晶体收集了分辨率为1.8 Å的完整数据集。
