Tandem repeat of a seven-bladed beta-propeller domain in oligoxyloglucan reducing-end-specific cellobiohydrolase

Structure
Katsuro YaoiYasushi Mitsuishi

Abstract

Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH; EC 3.2.1.150) is an exoglucanase that recognizes the reducing end of oligoxyloglucan and releases two glucosyl residue segments from the main chain. The X-ray crystal structure of OXG-RCBH determined at 2.2 A resolution reveals a unique feature of this enzyme; OXG-RCBH consists of a tandem repeat of two similar domains, which are both folded into seven-bladed beta-propeller structures. The sequence alignment of the propeller blades, based on the structure, indicates that a weak repeat of the amino acid sequence occurred seven times to construct each domain. There is a cleft that can accommodate the substrate oligosaccharide between the two domains, which is a putative substrate binding subsite. Mutation of either Asp35 or Asp465, located in the putative catalytic center, to Asn resulted in a protein with no detectable catalytic activity, indicating the critical role of these amino acids in catalysis.

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Citations

Dec 8, 2005·Applied and Environmental Microbiology·Katsuro YaoiYasushi Mitsuishi
Jun 1, 2013·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Evandro Ares de AraújoIgor Polikarpov
Sep 29, 2006·Pharmacology & Therapeutics·Christopher D KrauseSidney Pestka
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Jan 15, 2008·Neuropeptides·Alessandro Paiardini, Viviana Caputo
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Jul 29, 2011·The Journal of Biological Chemistry·Antonio ArizaGideon Davies
Jun 11, 2017·Scientific Reports·Fanny BoissierJorge Perez-Fernandez
Mar 25, 2021·Applied Microbiology and Biotechnology·Tomohiko MatsuzawaKatsuro Yaoi

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