@article {11019,
	title = {The Structure and Function of an Arabinan-specific alpha-1,2-Arabinofuranosidase Identified from Screening the Activities of Bacterial GH43 Glycoside Hydrolases},
	journal = {Journal of Biological Chemistry},
	volume = {286},
	number = {17},
	year = {2011},
	note = {Cartmell, Alan McKee, Lauren S. Pena, Maria J. Larsbrink, Johan Brumer, Harry Kaneko, Satoshi Ichinose, Hitomi Lewis, Richard J. Vikso-Nielsen, Anders Gilbert, Harry J. Marles-Wright, Jon},
	month = {04/2011},
	pages = {15483-15495},
	abstract = {Reflecting the diverse chemistry of plant cell walls, microorganisms that degrade these composite structures synthesize an array of glycoside hydrolases. These enzymes are organized into sequence-, mechanism-, and structure-based families. Genomic data have shown that several organisms that degrade the plant cell wall contain a large number of genes encoding family 43 (GH43) glycoside hydrolases. Here we report the biochemical properties of the GH43 enzymes of a saprophytic soil bacterium, Cellvibrio japonicus, and a human colonic symbiont, Bacteroides thetaiotaomicron. The data show that C. japonicus uses predominantly exo-acting enzymes to degrade arabinan into arabinose, whereas B. thetaiotaomicron deploys a combination of endo-and side chain-cleaving glycoside hydrolases. Both organisms, however, utilize an arabinan-specific alpha-1,2-arabinofuranosidase in the degradative process, an activity that has not previously been reported. The enzyme can cleave alpha-1,2-arabinofuranose decorations in single or double substitutions, the latter being recalcitrant to the action of other arabinofuranosidases. The crystal structure of the C. japonicus arabinan-specific alpha-1,2-arabinofuranosidase, CjAbf43A, displays a five-bladed beta-propeller fold. The specificity of the enzyme for arabinan is conferred by a surface cleft that is complementary to the helical backbone of the polysaccharide. The specificity of CjAbf43A for alpha-1,2-L-arabinofuranose side chains is conferred by a polar residue that orientates the arabinan backbone such that O2 arabinose decorations are directed into the active site pocket. A shelflike structure adjacent to the active site pocket accommodates O3 arabinose side chains, explaining how the enzyme can target O2 linkages that are components of single or double substitutions.},
	issn = {1083-351X},
	doi = {10.1074/jbc.M110.215962},
	author = {Cartmell, A. and McKee, L. S. and Pena, M. J. and Larsbrink, J. and Brumer, Harry and Kaneko, S. and Ichinose, H. and Lewis, R. J. and Vikso-Nielsen, A. and Gilbert, H. J. and Marles-Wright, J.}
}
