NDLI: Prediction of a common beta-propeller catalytic domain for fructosyltransferases of different origin and substrate specificity.

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Prediction of a common beta-propeller catalytic domain for fructosyltransferases of different origin and substrate specificity.

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Prediction of a common beta-propeller catalytic domain for fructosyltransferases of different origin and substrate specificity.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Hernández, L. Batista, F. R. Chinea, G. Pons, T.
Description	Country affiliation: Cuba Author Affiliation: Pons T ( Centro de Ingeniería Genética y Biotecnología (CIGB), Havana, Cuba. tirso.pons@cigb.edu.cu)
Abstract	The three-dimensional (3D) structure of fructan biosynthetic enzymes is still unknown. Here, we have explored folding similarities between reported microbial and plant enzymes that catalyze transfructosylation reactions. A sequence-structure compatibility search using TOPITS, SDP, 3D-PSSM, and SAM-T98 programs identified a beta-propeller fold with scores above the confidence threshold that indicate a structurally conserved catalytic domain in fructosyltransferases (FTFs) of diverse origin and substrate specificity. The predicted fold appeared related to that of neuraminidase and sialidase, of glycoside hydrolase families 33 and 34, respectively. The most reliable structural model was obtained using the crystal structure of neuraminidase (Protein Data Bank file: 5nn9) as template, and it is consistent with the location of previously identified functional residues of bacterial levansucrases (Batista et al., 1999; Song & Jacques, 1999). The sequence-sequence analysis presented here reinforces the recent inclusion of fungal and plant FTFs into glycoside hydrolase family 32, and suggests a modified sequence pattern H-x (2)-[PTV]-x (4)-[LIVMA]-[NSCAYG]-[DE]-P-[NDSC][GA]3 for this family.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	11
Volume Number	9
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2000-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Catalytic Domain Hexosyltransferases Chemistry Amino Acid Sequence Databases, Factual Models, Molecular Molecular Sequence Data Phylogeny Plant Proteins Protein Folding Sequence Homology, Amino Acid Substrate Specificity Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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