PubMed Journals: FEBS Lett

  Source:		PMID: 12387897

    		FEBS Lett. 2002 Oct 23;530(1-3):225-32.
			Beta-helical catalytic domains in glycoside
			hydrolase families 49, 55 and 87: domain
			architecture, modelling and assignment of
			catalytic residues.

			Rigden DJ(1), Franco OL.

			Author Information
			(1) Embrapa Genetic Resources and Biotechnology,
			Cenargen/Embrapa, S.A.I.N. Parque Rural,
			Final W5, Asa Norte, 70770-900 Brasília
			DF, Brazil. daniel@cenargen.embrapa.br

			X-ray crystallography and bioinformatics
			studies reveal a tendency for the right-handed
			beta-helix domain architecture to be associated
			with carbohydrate binding proteins. Here
			we demonstrate the presence of catalytic
			beta-helix domains in glycoside hydrolase
			(GH) families 49, 55 and 87 and provide
			evidence for their sharing a common evolutionary
			ancestor with two structurally characterized
			GH families, numbers 28 and 82. This domain
			assignment helps assign catalytic residues
			to each family. Further analysis of domain
			architecture reveals the association of
			carbohydrate binding modules with catalytic
			GH beta-helices, as well as an unexpected
			pair of beta-helix domains in GH family

			PMID: 12387897 [Indexed for MEDLINE]

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