Structural highlights
Function
Q973H2_SULTO
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The Sulfolobus tokodaii protein ST0929 shares close structural homology with S. acidocaldarius maltooligosyl trehalose synthase (SaMTSase), suggesting that the two enzymes share a common enzymatic mechanism. MTSase is one of a pair of enzymes that catalyze trehalose biosynthesis. The relative geometries of the ST0929 and SaMTSase active sites were found to be essentially identical. ST0929 also includes the unique tyrosine cluster that encloses the reducing-end glucose subunit in Sulfolobus sp. MTSases. The current structure provides insight into the structural basis of the increase in the hydrolase side reaction that is observed for mutants in which a phenylalanine residue is replaced by a tyrosine residue in the subsite +1 tyrosine cluster of Sulfolobus sp.
Structure of ST0929, a putative glycosyl transferase from Sulfolobus tokodaii.,Cielo CB, Okazaki S, Suzuki A, Mizushima T, Masui R, Kuramitsu S, Yamane T Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Apr 1;66(Pt 4):397-400., Epub 2010 Mar 26. PMID:20383007[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cielo CB, Okazaki S, Suzuki A, Mizushima T, Masui R, Kuramitsu S, Yamane T. Structure of ST0929, a putative glycosyl transferase from Sulfolobus tokodaii. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Apr 1;66(Pt 4):397-400., Epub 2010 Mar 26. PMID:20383007 doi:10.1107/S1744309110006354
