000078975 001__ 78975
000078975 005__ 20200716101429.0
000078975 0247_ $$2doi$$a10.1038/s41467-019-09674-0
000078975 0248_ $$2sideral$$a111406
000078975 037__ $$aART-2019-111406
000078975 041__ $$aeng
000078975 100__ $$aFang, W.
000078975 245__ $$aMechanisms of redundancy and specificity of the Aspergillus fumigatus Crh transglycosylases
000078975 260__ $$c2019
000078975 5060_ $$aAccess copy available to the general public$$fUnrestricted
000078975 5203_ $$aFungal cell wall synthesis is achieved by a balance of glycosyltransferase, hydrolase and transglycosylase activities. Transglycosylases strengthen the cell wall by forming a rigid network of crosslinks through mechanisms that remain to be explored. Here we study the function of the Aspergillus fumigatus family of five Crh transglycosylases. Although crh genes are dispensable for cell viability, simultaneous deletion of all genes renders cells sensitive to cell wall interfering compounds. In vitro biochemical assays and localisation studies demonstrate that this family of enzymes functions redundantly as transglycosylases for both chitin-glucan and chitin-chitin cell wall crosslinks. To understand the molecular basis of this acceptor promiscuity, we solved the crystal structure of A. fumigatus Crh5 (AfCrh5) in complex with a chitooligosaccharide at the resolution of 2.8 Å, revealing an extensive elongated binding cleft for the donor (-4 to -1) substrate and a short acceptor (+1 to +2) binding site. Together with mutagenesis, the structure suggests a “hydrolysis product assisted” molecular mechanism favouring transglycosylation over hydrolysis.
000078975 536__ $$9info:eu-repo/grantAgreement/ES/DGA/E34-R17$$9info:eu-repo/grantAgreement/ES/MINECO/BFU2016-75633-P$$9info:eu-repo/grantAgreement/ES/MINECO/BIO2016-79289-P$$9info:eu-repo/grantAgreement/ES/MINECO/CTQ2013-44367-C2-2-P
000078975 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000078975 590__ $$a12.121$$b2019
000078975 592__ $$a5.569$$b2019
000078975 591__ $$aMULTIDISCIPLINARY SCIENCES$$b6 / 71 = 0.085$$c2019$$dQ1$$eT1
000078975 593__ $$aBiochemistry, Genetics and Molecular Biology (miscellaneous)$$c2019$$dQ1
000078975 593__ $$aPhysics and Astronomy (miscellaneous)$$c2019$$dQ1
000078975 593__ $$aChemistry (miscellaneous)$$c2019$$dQ1
000078975 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000078975 700__ $$aSanz, A.B.
000078975 700__ $$aBartual, S.G.
000078975 700__ $$aWang, B.
000078975 700__ $$aFerenbach, A.T.
000078975 700__ $$aFarkaš, V.
000078975 700__ $$0(orcid)0000-0002-3122-9401$$aHurtado-Guerrero, R.$$uUniversidad de Zaragoza
000078975 700__ $$aArroyo, J.
000078975 700__ $$avan Aalten, D.M.F.
000078975 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000078975 773__ $$g10, 1 (2019), 1669$$pNATURE COMMUNICATIONS$$tNature Communications$$x2041-1723
000078975 8564_ $$s357907$$uhttps://zaguan.unizar.es/record/78975/files/texto_completo.pdf$$yVersión publicada
000078975 8564_ $$s69477$$uhttps://zaguan.unizar.es/record/78975/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000078975 909CO $$ooai:zaguan.unizar.es:78975$$particulos$$pdriver
000078975 951__ $$a2020-07-16-08:47:28
000078975 980__ $$aARTICLE