2.3.1.31	dimer	2 * 35000-40000, SDS-PAGE and electrospray ionization-mass spectrometry	486788	
2.3.1.31	dimer	MsHAT functions as a dimer. For dimerization, the alpha3 and alpha4 of the lid domain from each subunit form an antiparallel four-helix bundle with the hydrophobic core and the two helices from each subunit surround the dimerization center. In addition, the alpha5 and alpha5-alpha6 connecting loop extend to the other monomer and interact with residues from the other molecule through hydrogen bonds and salt bridges. The conformation of the alpha5 to alpha6 region might influence the shape of the dimer. The active site entrance shows an open or closed conformation and might determine the substrate binding affinity of HAT enzymes	-, 755982	
2.3.1.31	homodimer	2 * x, crystal structure with substrate L-homoserine	687796	
2.3.1.31	homodimer	crystal structure	684874	
2.3.1.31	monomer	1 * 37000, SDS-PAGE	486782	
2.3.1.31	additional information	the monomeric structure of MsHAT consists of two distinctive domains: a core domain (residues Met1-Ala176 and His287-Arg368) and a lid domain (Val177-Ser286). The core domain shows alpha/beta hydrolase fold and contains an eight-stranded parallel beta-sheet with four alpha-helices on one side and one alpha-helix on the opposite site. The lid domain is inserted between beta8 and alpha8 and is composed of five alpha-helices, and it mainly contributes to dimerization of MsHAT. MsHAT functions as a dimer	-, 755982