(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Alphaproteobacteria: NE > Rhodobacterales: NE > Rhodobacteraceae: NE > Halocynthiibacter: NE > Halocynthiibacter arcticus: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MTDPQFLTTETGRKIAYHLTEGKGPGVVFLGGFMSDMGGTKAVYLEEWAK KTGRAFLRFDYSGHGESSGVFTNGCIGEWAADAQAAISTLTEGPQILVGS SMGGWMALLVARAMPEKVAGLVGIAAAPDFTEDSMWGGFDAVQKVEMAET GRVALPSEYGDGPYIITRKLIEDGRENLVLRSPLSLPFPTRFLQGTADAD VDTSVAMRLLEHVEGGDVRLTLVKGADHRFSTPECLNLITKTCEKVIARA KF
This report deals with the purification, characterization, and a preliminary crystallographic study of a novel cold-active esterase (HaEst1) from Halocynthiibacter arcticus. Primary sequence analysis reveals that HaEst1 has a catalytic serine in G-x-S-x-G motif. The recombinant HaEst1 was cloned, expressed, and purified. SDS-PAGE and zymographic analysis were carried out to characterize the properties of HaEst1. A single crystal of HaEst1 was obtained in a solution containing 10% (w/v) PEG 8000/8% ethylene glycol, 0.1 M Hepes-NaOH, pH 7.5. Diffraction data were collected to 2.10 A resolution with P21 space group. The final Rmerge and Rp.i.m values were 7.6% and 3.5% for 50-2.10 A resolution. The unit cell parameters were a = 35.69 A, b = 91.21 A, c = 79.15 A, and beta = 96.9deg
