1e8q
From Proteopedia
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
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CHARACTERISATION OF THE CELLULOSE DOCKING DOMAIN FROM PIROMYCES EQUI
Overview
The recycling of photosynthetically fixed carbon in plant cell walls is a key microbial process. In anaerobes, the degradation is carried out by a high molecular weight multifunctional complex termed the cellulosome. This consists of a number of independent enzyme components, each of which contains a conserved dockerin domain, which functions to bind the enzyme to a cohesin domain within the protein scaffoldin protein. Here we describe the first three-dimensional structure of a fungal dockerin, the N-terminal dockerin of Cel45A from the anaerobic fungus Piromyces equi. The structure contains a novel fold of 42 residues. The ligand binding site consists of residues Trp 35, Tyr 8 and Asp 23, which are conserved in all fungal dockerins. The binding site is on the opposite side of the N- and C-termini of the molecule, implying that tandem dockerin domains, seen in the majority of anaerobic fungal plant cell wall degrading enzymes, could present multiple simultaneous binding sites and, therefore, permit tailoring of binding to catalytic demands.
About this Structure
1E8Q is a Single protein structure of sequence from Piromyces equi. Full crystallographic information is available from OCA.
Reference
Characterization of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi., Raghothama S, Eberhardt RY, Simpson P, Wigelsworth D, White P, Hazlewood GP, Nagy T, Gilbert HJ, Williamson MP, Nat Struct Biol. 2001 Sep;8(9):775-8. PMID:11524680
Page seeded by OCA on Sun Mar 30 19:57:36 2008
