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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003761naa a2200433 4500
001oai:DiVA.org:kth-179862
003SwePub
008160104s2012 | |||||||||||000 ||eng|
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-1798622 URI
0247 a https://doi.org/10.1073/pnas.11176861092 DOI
040 a (SwePub)kth
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a McKee, Lauren,d 1985-u Newcastle University, United Kingdom; University of Georgia, United States4 aut0 (Swepub:kth)u1nbm728
2451 0a Introducing endo-xylanase activity into an exo-acting arabinofuranosidase that targets side chains
264 c 2012-04-06
264 1b NATIONAL ACADEMY OF SCIENCES,c 2012
338 a print2 rdacarrier
500 a QC 20160126
520 a The degradation of the plant cell wall by glycoside hydrolases is central to environmentally sustainable industries. The major polysaccharides of the plant cell wall are cellulose and xylan, a highly decorated beta-1,4-xylopyranose polymer. Glycoside hydrolases displaying multiple catalytic functions may simplify the enzymes required to degrade plant cell walls, increasing the industrial potential of these composite structures. Here we test the hypothesis that glycoside hydrolase family 43 (GH43) provides a suitable scaffold for introducing additional catalytic functions into enzymes that target complex structures in the plant cell wall. We report the crystal structure of Humicola insolens AXHd3 (HiAXHd3), a GH43 arabinofuranosidase that hydrolyses O3-linked arabinose of doubly substituted xylans, a feature of the polysaccharide that is recalcitrant to degradation. HiAXHd3 displays an N-terminal five-bladed beta-propeller domain and a C-terminal beta-sandwich domain. The interface between the domains comprises a xylan binding cleft that houses the active site pocket. Substrate specificity is conferred by a shallow arabinose binding pocket adjacent to the deep active site pocket, and through the orientation of the xylan backbone. Modification of the rim of the active site introduces endo-xylanase activity, whereas the resultant enzyme variant, Y166A, retains arabinofuranosidase activity. These data show that the active site of HiAXHd3 is tuned to hydrolyse arabinofuranosyl or xylosyl linkages, and it is the topology of the distal regions of the substrate binding surface that confers specificity. This report demonstrates that GH43 provides a platform for generating bespoke multifunctional enzymes that target industrially significant complex substrates, exemplified by the plant cell wall.
650 7a LANTBRUKSVETENSKAPERx Bioteknologi med applikationer på växter och djurx Växtbioteknologi0 (SwePub)404012 hsv//swe
650 7a AGRICULTURAL SCIENCESx Agricultural Biotechnologyx Plant Biotechnology0 (SwePub)404012 hsv//eng
7001 a Pena, Maria J.4 aut
7001 a Rogowski, Artur4 aut
7001 a Jackson, Adam4 aut
7001 a Lewis, Richard J.4 aut
7001 a York, William S.4 aut
7001 a Krogh, Kristian B. R. M.4 aut
7001 a Vikso-Nielsen, Anders4 aut
7001 a Skjot, Michael4 aut
7001 a Gilbert, Harry J.4 aut
7001 a Marles-Wright, Jon4 aut
7102 a Newcastle University, United Kingdom; University of Georgia, United States4 org
7730 t Proceedings of the National Academy of Sciences of the United States of Americad : NATIONAL ACADEMY OF SCIENCESg 109:17q 109:17x 0027-8424x 1091-6490
8564 u https://www.pnas.org/content/pnas/109/17/6537.full.pdf
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-179862
8564 8u https://doi.org/10.1073/pnas.1117686109

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