The X-ray crystallographic structure of Escherichia coli branching enzyme

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dc.contributor.authorAbad, M. C.
dc.contributor.authorBinderup, K.
dc.contributor.authorRios-Steiner, J.
dc.contributor.authorArni, R. K.
dc.contributor.authorPreiss, J.
dc.contributor.authorGeiger, J. H.
dc.contributor.institutionMichigan State University
dc.contributor.institutionUniv Puerto Rico
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T14:02:22Z
dc.date.available2014-05-20T14:02:22Z
dc.date.issued2002-11-01
dc.description.abstractBranching enzyme catalyzes the formation of alpha-1,6 branch points in either glycogen or starch. We report the 2.3-Angstrom crystal structure of glycogen branching enzyme from Escherichia coli. The enzyme consists of three major domains, an NH2-terminal seven-stranded beta-sandwich domain, a COOH-terminal domain, and a central alpha/beta-barrel domain containing the enzyme active site. While the central domain is similar to that of all the other amylase family enzymes, branching enzyme shares the structure of all three domains only with isoamylase. Oligosaccharide binding was modeled or branching enzyme using the enzyme-oligosaccharide complex structures of various alpha-amylases and cyclodextrin glucanotransferase and residues were implicated in oligosaccharide binding. While most of the oligosaccharides modeled well in the branching enzyme structure, an approximate 50degrees rotation between two of the glucose units was required to avoid steric clashes with Trp(298) of branching enzyme. A similar rotation was observed in the mammalian alpha-amylase structure caused by an equivalent tryptophan residue in this structure. It appears that there are two binding modes for oligosaccharides in these structures depending on the identity and location of this aromatic residue.en
dc.description.affiliationMichigan State Univ, Dept Chem, E Lansing, MI 48824 USA
dc.description.affiliationMichigan State Univ, Dept Biochem & Mol Biol, E Lansing, MI 48824 USA
dc.description.affiliationUniv Puerto Rico, Dept Chem, Mayaguez, PR 00681 USA
dc.description.affiliationUNESP, IBILCE, Dept Phys, BR-15054400 Sao Jose Dos Campos, SP, Brazil
dc.description.affiliationUnespUNESP, IBILCE, Dept Phys, BR-15054400 Sao Jose Dos Campos, SP, Brazil
dc.format.extent42164-42170
dc.identifierhttp://dx.doi.org/10.1074/jbc.M205746200
dc.identifier.citationJournal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc., v. 277, n. 44, p. 42164-42170, 2002.
dc.identifier.doi10.1074/jbc.M205746200
dc.identifier.issn0021-9258
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/21984
dc.identifier.wosWOS:000178985300109
dc.language.isoeng
dc.publisherAmer Soc Biochemistry Molecular Biology Inc
dc.relation.ispartofJournal of Biological Chemistry
dc.relation.ispartofjcr4.010
dc.relation.ispartofsjr2,672
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.titleThe X-ray crystallographic structure of Escherichia coli branching enzymeen
dc.typeArtigo
dcterms.licensehttp://www.jbc.org/site/misc/Copyright_Permission.xhtml
dcterms.rightsHolderAmer Soc Biochemistry Molecular Biology Inc
unesp.author.lattes9162508978945887[4]
unesp.author.orcid0000-0003-2460-1145[4]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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