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The O-Glycosylated Linker from the Trichoderma reesei Family 7 Cellulase Is a Flexible, Disordered Protein
Vise andre og tillknytning
2010 (engelsk)Inngår i: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 99, nr 11, s. 3773-3781Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Fungi and bacteria secrete glycoprotein cocktails to deconstruct cellulose Cellulose degrading enzymes (cellulases) are often modular with catalytic domains for cellulose hydrolysis and carbohydrate binding modules connected by linkers rich in serine and threonine with O-glycosylation Few studies have probed the role that the linker and O-glycans play in catalysis Since different expression and growth conditions produce different glycosylation patterns that affect enzyme activity the structure function relationships that glycosylation imparts to linkers are relevant for understanding cellulase mechanisms Here the linker of the Trichoderma reesei Family 7 cellobiohydrolase (Cel7A) is examined by simulation Our results suggest that the Cel7A linker is an intrinsically disordered protein with and without glycosylation Contrary to the predominant view the O-glycosylation does not change the stiffness of the linker as measured by the relative fluctuations in the end to end distance rather it provides a 16 A extension thus expanding the operating range of Cel7A We explain observations from previous biochemical experiments in the light of results obtained here and compare the Cel7A linker with linkers from other cellulases with sequence based tools to predict disorder This preliminary screen indicates that linkers from Family 7 enzymes from other genera and other cellulases within T reesei may not be as disordered warranting further study

sted, utgiver, år, opplag, sider
2010. Vol. 99, nr 11, s. 3773-3781
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Identifikatorer
URN: urn:nbn:se:kth:diva-27982DOI: 10.1016/j.bpj.2010.10.032ISI: 000285033800030Scopus ID: 2-s2.0-78649852734OAI: oai:DiVA.org:kth-27982DiVA, id: diva2:382700
Merknad
QC 20110103Tilgjengelig fra: 2011-01-03 Laget: 2011-01-03 Sist oppdatert: 2017-12-11bibliografisk kontrollert

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