3HJE

Crystal structure of sulfolobus tokodaii hypothetical maltooligosyl trehalose synthase

Summary for 3HJE

• Entry DOI: 10.2210/pdb3hje/pdb
• Descriptor: 704aa long hypothetical glycosyltransferase, GLYCEROL (3 entities in total)
• Functional Keywords: trehalose biosynthesis, maltooligoside trehalose synthase (mtsase), family 13 glycoside hydrolases, sulfolobus tokodaii, tyrosine cluster, transferase
• Biological source: Sulfolobus tokodaii str. 7
• Total number of polymer chains: 1
• Total formula weight: 84097.96

Authors

Cielo, C.B.C.,Okazaki, S.,Suzuki, A.,Mizushima, T.,Masui, R.,Kuramitsu, S.,Yamane, T. (deposition date: 2009-05-21, release date: 2010-04-14, Last modification date: 2024-10-30)

Primary citation

Cielo, C.B.C.,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, 66:397-400, 2010

PubMed Abstract: 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.

PubMed: 20383007
DOI: 10.1107/S1744309110006354

Experimental method

X-RAY DIFFRACTION (1.9 Å)