Characterization of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi.

摘要: The recycling of photosynthetically fixed carbon in plant cell walls is a key microbial process. In anaerobes, the degradation carried out by high molecular weight multifunctional complex termed cellulosome. This consists number independent enzyme components, each which contains conserved dockerin domain, functions to bind cohesin domain within protein scaffoldin protein. Here we describe first three-dimensional structure fungal dockerin, N-terminal Cel45A from anaerobic fungus Piromyces equi. novel fold 42 residues. ligand binding site residues Trp 35, Tyr 8 and Asp 23, are all dockerins. on opposite side N- C-termini molecule, implying that tandem domains, seen majority wall degrading enzymes, could present multiple simultaneous sites and, therefore, permit tailoring catalytic demands.