Structural Insights Into The Beta-mannosidase From T. Reesei Obtained By Synchrotron Small-angle X-ray Solution Scattering Enhanced By X-ray Crystallography.

dc.creatorAparicio, Ricardo
dc.creatorFischer, Hannes
dc.creatorScott, David J
dc.creatorVerschueren, Koen H G
dc.creatorKulminskaya, Anna A
dc.creatorEneiskaya, Elena V
dc.creatorNeustroev, Kirill N
dc.creatorCraievich, Aldo Felix
dc.creatorGolubev, Alexander M
dc.creatorPolikarpov, Igor
dc.date2002-Jul
dc.date2015-11-27T12:49:10Z
dc.date2015-11-27T12:49:10Z
dc.date.accessioned2018-03-29T00:56:19Z
dc.date.available2018-03-29T00:56:19Z
dc.identifierBiochemistry. v. 41, n. 30, p. 9370-5, 2002-Jul.
dc.identifier0006-2960
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/12135358
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/195096
dc.identifier12135358
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1295329
dc.descriptionA molecular envelope of the beta-mannosidase from Trichoderma reesei has been obtained by combined use of solution small-angle X-ray scattering (SAXS) and protein crystallography. Crystallographic data at 4 A resolution have been used to enhance informational content of the SAXS data and to obtain an independent, more detailed protein shape. The phased molecular replacement technique using a low resolution SAXS model, building, and refinement of a free atom model has been employed successfully. The SAXS and crystallographic free atom models exhibit a similar globular form and were used to assess available crystallographic models of glycosyl hydrolases. The structure of the beta-galactosidase, a member of a family 2, clan GHA glycosyl hydrolases, shows an excellent fit to the experimental molecular envelope and distance distribution function of the beta-mannosidase, indicating gross similarities in their three-dimensional structures. The secondary structure of beta-mannosidase quantified by circular dichroism measurements is in a good agreement with that of beta-galactosidase. We show that a comparison of distance distribution functions in combination with 1D and 2D sequence alignment techniques was able to restrict the number of possible structurally homologous proteins. The method could be applied as a general method in structural genomics and related fields once protein solution scattering data are available.
dc.description41
dc.description9370-5
dc.languageeng
dc.relationBiochemistry
dc.relationBiochemistry
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectCircular Dichroism
dc.subjectCrystallography, X-ray
dc.subjectMannosidases
dc.subjectProtein Conformation
dc.subjectProtein Folding
dc.subjectScattering, Radiation
dc.subjectTrichoderma
dc.subjectBeta-mannosidase
dc.titleStructural Insights Into The Beta-mannosidase From T. Reesei Obtained By Synchrotron Small-angle X-ray Solution Scattering Enhanced By X-ray Crystallography.
dc.typeArtículos de revistas


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