In addition, we report that this enzyme crystallizes in the inactive conformation, which is a first observation among more than 55 crystal structures reported so far. Glycosylation is an important process in the biofilm formation during the infection of Streptococcus pneumoniae establishing the fact that post-translational glycosylation of proteins in this organism is critical. In addition to glycosylation, tyrosine phosphorylation is also an essential post-translational modification for capsid formation of streptococci family. The 27 amino acid insert in the streptococcal MetAP1a with possible glycosylation and phosphorylation modifications structurally aligns well with P-X-X-P motif region of Type Ib and Type Ic, suggesting important functions apart from removal of the initiator methionine. One possibility is that it could be useful in localization to a specific region in the cell for example to the cell membrane or to the ribosomes. In addition, it may also be involved in some signaling cascade. Though, it is not obvious from the sequence, due to the glycosylation or phosphorylation, if this protein is exported to the cell surface, the unique sequence of the extra-region of streptococcal MetAPs can be used as an antigen to develop vaccine against some of the deadly streptococcal strains. This is the first crystal structure of MetAP determined in the closed/inactive conformation. However, the enzyme is active in solution showing strict specificity to methionine containing peptides. The flip of the beta-hairpin into the active site results in the occlusion of the methionine into the active site. This could be due to the crystal-packing artifact or it could be a representation of physiological AbMole Gambogic-acid switch between active and inactive forms induced 
by the two new insert regions, which are in close proximity to the active site. There are more than 55 structures of various MetAPs deposited in the protein databank AbMole Oxytocin Syntocinon crystallized in different space groups and none of them displayed inactive/closed conformation. In addition, activity on the crystals point that these loops are not flexible in the crystal form. The conventional method to measure the NF-kB activity is the electrophoretic mobility shift assay. However, it is a laborious and time-consuming procedure that typically requires the use of radioactive probes and antibodies against NF-kBs. Luciferase reporter assays have also been used to detect the DNA binding and transcriptional activity. These assays, however, are difficult to apply in high-throughput screening of clinical samples. Renard and colleagues established a more convenient DNA binding assay on the basis of a modified enzyme-linked immunosorbent assay. However, this assay is unfit for emergency tests such as evaluating the degree of acute inflammation because it requires at least three hours for the assay time.