5.3.1.23	dimer	-	662258	
5.3.1.23	dimer	x-ray crystallography	695004	
5.3.1.23	homodimer	2 * 38900, detagged recombinant enzyme, SDS-PAGE	-, 760727	
5.3.1.23	homodimer	2 * 40000, about, recombinant enzyme, SDS-PAGE	761764	
5.3.1.23	additional information	enzyme structure and active site structure comparisons, open/closed conformational transition of enzyme M1Pi. The structure of Bs-M1Pi shows that the active site is completely shielded from the solvent region. The substrate binding is likely to induce the large conformational changes of N- and C-terminal domains as well as the rearrangement of the hydrogen-bond network around the loops 93-98 and 290-294 to stabilize the closed state of the enzyme	-, 762331	
5.3.1.23	additional information	enzyme three-dimensional structure analysis and structure comparisons. The most visible difference between the open and closed conformation can be perceived in the position of the loop connecting the helices alpha3 and alpha4 of the NTD. In the open state, the loop is away from the active-site pocket, whereas in the closed state the loop moves toward the active-site pocket with a forward shift of about 24 A	761764