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4V39

Apo-structure of alpha2,3-sialyltransferase variant 2 from Pasteurella dagmatis

Summary for 4V39
Entry DOI10.2210/pdb4v39/pdb
Related4V2U 4V38 4V3B 4V3C
DescriptorSIALYLTRANSFERASE (2 entities in total)
Functional Keywordstransferase
Biological sourcePASTEURELLA DAGMATIS
Total number of polymer chains1
Total formula weight45642.94
Authors
Pavkov-Keller, T.,Schmoelzer, K.,Czabany, T.,Luley-Goedl, C.,Ribitsch, D.,Schwab, H.,Nidetzky, B.,Gruber, K. (deposition date: 2014-10-17, release date: 2015-04-08, Last modification date: 2024-01-10)
Primary citationSchmoelzer, K.,Czabany, T.,Pavkov-Keller, T.,Luley-Goedl, C.,Ribitsch, D.,Schwab, H.,Gruber, K.,Nidetzky, B.
Complete Switch from Alpha2,3- to Alpha2,6-Regioselectivity in Pasteurella Dagmatis Beta-D-Galactoside Sialyltransferase by Active-Site Redesign
Chem.Commun.(Camb.), 51:3083-, 2015
Cited by
PubMed Abstract: Structure-guided active-site redesign of a family GT-80 β-D-galactoside sialyltransferase (from Pasteurella dagmatis) to change enzyme regioselectivity from α-2,3 in the wild type to α-2,6 in a P7H-M117A double mutant is reported. Biochemical data for sialylation of lactose together with protein crystal structures demonstrate highly precise enzyme engineering.
PubMed: 25619424
DOI: 10.1039/C4CC09772F
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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