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Curr Opin Struct Biol. 2016 Oct;40:23-32. doi: 10.1016/j.sbi.2016.07.007. Epub 2016 Jul 21.

The conformational plasticity of glycosyltransferases.

Author information

1
Structural Biology Unit, CIC bioGUNE, Bizkaia Technology Park, 48160 Derio, Spain; Unidad de Biofísica, Centro Mixto Consejo Superior de Investigaciones Científicas, Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC, UPV/EHU), Barrio Sarriena s/n, Leioa, Bizkaia 48940, Spain; Departamento de Bioquímica, Universidad del País Vasco, Leioa, Bizkaia 48940, Spain; IKERBASQUE, Basque Foundation for Science, 48011 Bilbao, Spain.
2
Structural Biology Unit, CIC bioGUNE, Bizkaia Technology Park, 48160 Derio, Spain; Unidad de Biofísica, Centro Mixto Consejo Superior de Investigaciones Científicas, Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC, UPV/EHU), Barrio Sarriena s/n, Leioa, Bizkaia 48940, Spain; Departamento de Bioquímica, Universidad del País Vasco, Leioa, Bizkaia 48940, Spain; IKERBASQUE, Basque Foundation for Science, 48011 Bilbao, Spain. Electronic address: mrcguerin@cicbiogune.es.

Abstract

Glycosyltransferases (GTs) catalyze the transfer of a sugar moiety from nucleotide-sugar or lipid-phospho-sugar donors to a broad range of acceptor substrates, generating a significant amount of structural diversity in biological systems. GTs are highly selective in nature, allowing the recognition of subtle structural differences in the sequences and stereochemistry of their sugar and acceptor substrates. To achieve the enzyme-transition state complex, a particular spatial arrangement of the active site is required, highlighting the importance of protein dynamics, conformational changes and plasticity of GTs during substrate recognition and catalysis. The elucidations of the molecular mechanisms by which these events govern the function and substrate specificity of GTs represent a major challenge.

PMID:
27450114
DOI:
10.1016/j.sbi.2016.07.007
[Indexed for MEDLINE]

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