ACTIVE SITE ARCHITECTURE OF DISPERSIN B, A BETA-HEXOSAMINIDASE

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. We have solved the crystal structure of dispersin B at 2.0 A resolution. Our current project focuses on the detremination of active ste residues and their role in hydrolysis. We have made several mutants of this enzyme based on the sequence similarity of the enzyme with other beta-hexosaminidases. We would now like to identify the various subites present in this molecule. Our initial efforts will focus on the co-crystallization of N-acetylglucosamine anf the mutant enzymes. Our initial stuidies have produced crystals that diffract upto 2.7A. However, the active site has a bound acetate that prevents N-acetylglucosamine to occupy the active only partially. Since the crystals are small, we feel that collecting data at the beam line should increase the resolution. The high resolution data would be of great use for our studies.