Structural basis for branching-enzyme activity of glycoside hydrolase family 57: Structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus Kodakaraensis KOD1

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dc.contributor.authorSantos, Camila R.
dc.contributor.authorTonoli, Celisa C. C.
dc.contributor.authorTrindade, Daniel M.
dc.contributor.authorBetzel, Christian
dc.contributor.authorTakata, Hiroki
dc.contributor.authorKuriki, Takashi
dc.contributor.authorKanai, Tamotsu
dc.contributor.authorImanaka, Tadayuki
dc.contributor.authorArni, Raghuvir K. [UNESP]
dc.contributor.authorMurakami, Mario T.
dc.contributor.institutionNatl Ctr Res Energy & Mat
dc.contributor.institutionUniv Hamburg
dc.contributor.institutionEzaki Glico Co Ltd
dc.contributor.institutionKyoto Univ
dc.contributor.institutionRitsumeikan Univ
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T14:02:36Z
dc.date.available2014-05-20T14:02:36Z
dc.date.issued2011-02-01
dc.description.abstractBranching enzymes (BEs) catalyze the formation of branch points in glycogen and amylopectin by cleavage of alpha-1,4 glycosidic bonds and subsequent transfer to a new alpha-1,6 position. BEs generally belong to glycoside hydrolase family 13 (GH13); however TK1436, isolated from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1, is the first GH57 member, which possesses BE activity. To date, the only BE structure that had been determined is a GH13-type from Escherichia coli. Herein, we have determined the crystal structure of TK1436 in the native state and in complex with glucose and substrate mimetics that permitted mapping of the substrate-binding channel and identification of key residues for glucanotransferase activity. Its structure encompasses a distorted (beta/alpha)(7)-barrel juxtaposed to a C-terminal alpha-helical domain, which also participates in the formation of the active-site cleft. The active site comprises two acidic catalytic residues (Glu183 and Asp354), the polarizer His 10, aromatic gate-keepers (Trp28, Trp270, Trp407, and Trp416) and the residue Tyr233, which is fully conserved among GH13- and GH57-type BEs. Despite TK1436 displaying a completely different fold and domain organization when compared to E. coli BE, they share the same structural determinants for BE activity. Structural comparison with AmyC, a GH57 alpha-amylase devoid of BE activity, revealed that the catalytic loop involved in substrate recognition and binding, is shortened in AmyC structure and it has been addressed as a key feature for its inability for glucanotransferase activity. The oligomerization has also been pointed out as a possible determinant for functional differentiation among GH57 members. Proteins 2011; 79:547-557. (C) 2010 Wiley-Liss, Inc.en
dc.description.affiliationNatl Ctr Res Energy & Mat, Natl Lab Biosci, Campinas, SP, Brazil
dc.description.affiliationUniv Hamburg, Inst Biochem & Mol Biol, Hamburg, Germany
dc.description.affiliationEzaki Glico Co Ltd, Inst Hlth Sci, Osaka, Japan
dc.description.affiliationKyoto Univ, Grad Sch Engn, Dept Synthet Chem & Biol Chem, Kyoto, Japan
dc.description.affiliationRitsumeikan Univ, Coll Life Sci, Dept Biotechnol, Kusatsu, Japan
dc.description.affiliationState Univ São Paulo, Dept Phys, Sao Jose do Rio Preto, Brazil
dc.description.affiliationUnespState Univ São Paulo, Dept Phys, Sao Jose do Rio Preto, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent547-557
dc.identifierhttp://dx.doi.org/10.1002/prot.22902
dc.identifier.citationProteins-structure Function and Bioinformatics. Malden: Wiley-blackwell, v. 79, n. 2, p. 547-557, 2011.
dc.identifier.doi10.1002/prot.22902
dc.identifier.issn0887-3585
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/22069
dc.identifier.wosWOS:000286905600017
dc.language.isoeng
dc.publisherWiley-Blackwell
dc.relation.ispartofProteins: Structure, Function and Bioinformatics
dc.relation.ispartofjcr2.274
dc.relation.ispartofsjr1,362
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectglycoside hydrolase family 57en
dc.subjectbranching enzymeen
dc.subjectCrystal structureen
dc.subjectcatalytic mechanismen
dc.titleStructural basis for branching-enzyme activity of glycoside hydrolase family 57: Structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus Kodakaraensis KOD1en
dc.typeArtigo
dcterms.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dcterms.rightsHolderWiley-blackwell
unesp.author.lattes9162508978945887[9]
unesp.author.orcid0000-0003-2460-1145[9]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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