Fold-recognition and comparative modeling of human alpha2,3-sialyltransferases reveal their sequence and structural similarities to CstII from Campylobacter jejuni.

BMC Structural Biology
M S Sujatha, Petety V Balaji

Abstract

The 3-D structure of none of the eukaryotic sialyltransferases (SiaTs) has been determined so far. Sequence alignment algorithms such as BLAST and PSI-BLAST could not detect a homolog of these enzymes from the protein databank. SiaTs, thus, belong to the hard/medium target category in the CASP experiments. The objective of the current work is to model the 3-D structures of human SiaTs which transfer the sialic acid in alpha2,3-linkage viz., ST3Gal I, II, III, IV, V, and VI, using fold-recognition and comparative modeling methods. The pair-wise sequence similarity among these six enzymes ranges from 41 to 63%. Unlike the sequence similarity servers, fold-recognition servers identified CstII, a alpha2,3/8 dual-activity SiaT from Campylobacter jejuni as the homolog of all the six ST3Gals; the level of sequence similarity between CstII and ST3Gals is only 15-20% and the similarity is restricted to well-characterized motif regions of ST3Gals. Deriving template-target sequence alignments for the entire ST3Gal sequence was not straightforward: the fold-recognition servers could not find a template for the region preceding the L-motif and that between the L- and S-motifs. Multiple structural templates were identified to model these reg...Continue Reading

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Citations

Nov 26, 2010·Glycobiology·Magali AudryChristelle Breton
Sep 30, 2016·Medicinal Research Reviews·Rémi Szabo, Danielle Skropeta
Mar 20, 2008·Biochemical and Biophysical Research Communications·Yihua Gu, Robert K Yu
Jul 16, 2008·Current Opinion in Chemical Biology·Alejandro Buschiazzo, Pedro M Alzari

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Software Mentioned

GeneSilico
PHYRE
Colorado3D
TMHMM
Tcoffee
PROCHECK
T99
T02
SSPRO
Modeller

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